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nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
mechanism
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
electron transfer from c heme to d1 heme is very slow, order of seconds
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
electron-transfer mechanism
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
rate constants of intermolecular electron transfer
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
proposed reaction mechanism
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
a copper protein, cytochrome c-552 or cytochrome c-553 from Pseudomonas denitrificans acts as acceptor
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
ordered mechanism in which electron transfer is gated by binding of nitrite to the type 2 Cu centre
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
reaction mechanism, overview. Mobility of two residues essential to catalytic activity, Asp98 and His244, are sterically restricted in GtNIR by Phe109 on a characteristic loop structure that is found above Asp98 and by an unusually short CH-O hydrogen bond observed between His244 and water, respectively. Analysis of the hydrogen-bond networks around His244 and the flow path of protons consumed by nitrite reduction. The electron transfer reaction is coupled with the proton transfer reaction
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
reaction mechanism, overview. The transformation from the initial O-coordination of substrate to the final N-coordination of product is achieved by electron transfer from T1 copper to T2 copper, rather than by the previously reported side-on coordination of a NO intermediate, which only takes place in the reduced enzyme. Role of structural change in the critical residue Asp98, which affects the energetics of substrate attachment and product release at the T2 copper reaction center, while it does not significantly affect the activation energy and reaction pathways of the nitrite reduction process
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
the proposed mechanisms for the reduction of nitrite by CuNiRs include intramolecular electron and proton transfers, proton-coupled electron transfer is one of the key processes in enzyme reactions, density functional theory calculations analysis. The reduction of T2 Cu site promotes the proton transfer, and the hydrogen bond network around the binding site has an important role not only to stabilize the nitrite binding but also to promote the proton transfer to nitrite. Reaction mechanism, overview
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
-
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
-
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
-
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
-
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
-
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
-
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
-
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
the proposed mechanisms for the reduction of nitrite by CuNiRs include intramolecular electron and proton transfers, proton-coupled electron transfer is one of the key processes in enzyme reactions, density functional theory calculations analysis. The reduction of T2 Cu site promotes the proton transfer, and the hydrogen bond network around the binding site has an important role not only to stabilize the nitrite binding but also to promote the proton transfer to nitrite. Reaction mechanism, overview
-
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
reaction mechanism, overview. Mobility of two residues essential to catalytic activity, Asp98 and His244, are sterically restricted in GtNIR by Phe109 on a characteristic loop structure that is found above Asp98 and by an unusually short CH-O hydrogen bond observed between His244 and water, respectively. Analysis of the hydrogen-bond networks around His244 and the flow path of protons consumed by nitrite reduction. The electron transfer reaction is coupled with the proton transfer reaction
-
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
-
-
-
-
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ferrocytochrome c + O2
ferricytochrome c + H2O
ferrocytochrome c-551 + NO2-
NO + ferricytochrome c-551
ferrocytochrome c-551 + O2
ferricytochrome c-551 + H2O
ferrocytochrome c-551 + O2
H2O + ferricytochrome c-551
hydroxylamine + reduced pseudoazurin
NH3 + H2O + oxidized pseudoazurin
-
-
-
-
?
N,N-dimethyl-p-phenylenediamine + oxidized benzyl viologen
?
-
-
-
-
?
NH2OH + NaNO2
N2O + H2O
-
-
-
?
NH2OH + reduced cytochrome c550
NH3 + H2O + oxidized cytochrome c550
-
additional electron donor: horse heart cytochrome c
-
?
nitric oxide + H2O + ferricytochrome c
nitrite + ferrocytochrome c + 2 H+
Marinobacter nauticus
-
-
-
-
?
nitric oxide + H2O + ferricytochrome c
nitrite + ferrocytochrome c + H+
nitric oxide + H2O + ferricytochrome c B0428
nitrite + ferrocytochrome c B0428 + 2 H+
-
-
-
?
nitric oxide + H2O + ferricytochrome c551
nitrite + ferrocytochrome c551 + 2 H+
-
-
-
?
nitric oxide + H2O + ferricytochrome c551
nitrite + ferrocytochrome c551 + H+
nitric oxide + H2O + ferricytochrome c552
nitrite + ferrocytochrome c552 + 2 H+
Marinobacter nauticus
-
-
-
-
?
nitric oxide + H2O + oxidized phenazine methosulfate
nitrite + reduced phenazine methosulfate + 2 H+
Marinobacter nauticus
-
phenazine methosulfate can serve as reducing agents and trigger catalytic activity if the assay is performed in relatively long time windows
-
-
?
nitric oxide + H2O + oxidized phenosafranin
nitrite + reduced phenosafranin + 2 H+
Marinobacter nauticus
-
phenosafranin can serve as reducing agents and trigger catalytic activity if the assay is performed in relatively long time windows
-
-
?
nitrite + dithionite
NO + reduced dithionite
-
type 1 copper of the fully loaded protein is reduced both directly by dithionite and indirectly by the type 2 copper site via intramolecular electron transfer
-
-
?
nitrite + electron donor
NO + oxidized electron donor
-
-
-
-
?
nitrite + electron donor
NO + oxidized electron donor + H2O
nitrite + ferrocytochrome b5 + 2 H+
nitric oxide + H2O + ferricytochrome b5
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
nitrite + ferrocytochrome c(gamma)
NO + H2O + ferricytochrome c(gamma)
-
-
-
-
?
nitrite + ferrocytochrome c2
NO + H2O + ferricytochrome c2
nitrite + ferrocytochrome c550
NO + ferricytochrome c550
-
-
-
-
?
nitrite + ferrocytochrome c550
NO + oxidized ferricytochrome c550
nitrite + ferrocytochrome V(gamma) + H+
nitric oxide + H2O + ferricytochrome V(gamma)
-
-
-
-
r
nitrite + H2O + reduced cytochrome cd1
nitric oxide + H+ + cytochrome cd1
anaerobic assay conditions
-
-
?
nitrite + H2O + reduced pseudoazurin
nitric oxide + H+ + pseudoazurin
nitrite + methyl viologen
NO + oxidized methyl viologen + H2O
-
-
-
?
nitrite + reduced ascorbate
nitric oxide + oxidized ascorbate
-
-
-
-
r
nitrite + reduced azurin
NO + H2O + oxidized azurin
nitrite + reduced azurin
NO + oxidized azurin
-
azurin purified from Pseudomonas chlororaphis
-
-
?
nitrite + reduced azurin I
NO + azurin I
-
-
-
?
nitrite + reduced azurin I
NO + oxidized azurin I
nitrite + reduced benzyl viologen
nitric oxide + oxidized benzyl viologen
-
-
-
-
?
nitrite + reduced benzyl viologen
NO + H2O + oxidized benzyl viologen
nitrite + reduced benzyl viologen
NO + oxidized benzyl viologen
nitrite + reduced benzyl viologen + 2 H+
nitric oxide + H2O + oxidized benzyl viologen
nitrite + reduced electron donor
NO + H2O + oxidized electron donor
nitrite + reduced hydroquinone
nitric oxide + H2O + hydroquinone
nitrite + reduced methyl viologen
NO + oxidized methyl viologen
-
random sequential mechanism
-
-
?
nitrite + reduced methyl viologen
NO + oxidized methyl viologen + H2O
nitrite + reduced phenazine methosulfate
NO + oxidized phenazine methosulfate
nitrite + reduced pseudoazurin
NO + H2O + oxidized pseudoazurin
-
-
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
nitrite + reduced pseudoazurin + H+
nitric oxide + oxidized pseudoazurin + H2O
NO2 + reduced methyl viologen
NO + oxidized methylviologen
-
-
-
?
NO2- + ferrocytochrome c
NO + ferricytochrome c
NO2- + morpholine
N-nitrosomorpholine
-
in the presence of diethyldithiocarbamic acid ethylester, nitrosation through the production of NO or NO+-like species
-
?
NO2- + Na2S2O4
NO + Na2S2O3
-
pysiological electron donor is unknown, no activity with methyl viologen, phenazine methosulfate or N,N,N',N',-tetramethyl-p-phenylenediamine
-
?
NO2- + reduced ascorbate
NO + oxidized ascorbate
NO2- + reduced azurin
NO + oxidized azurin
-
putative physiological electron donor
-
?
NO2- + reduced cytochrome c550
NO + oxidized cytochrome c550
-
unambiguously identified as physiological electron donor
-
?
NO2- + reduced pseudoazurin
NO + oxidized pseudoazurin
O2 + ferrocytochrome c
H2O + ferricytochrome c
O2 + reduced pseudoazurin
H2O + oxidized pseudoazurin
-
-
-
-
?
O2-. + H+
H2O2 + O2
-
purified enzyme shows superoxide dismutase activity, approx. one-third that of pure superoxide dismutase
-
?
reduced azurin + O2
oxidized azurin + H2O
reduced tetramethyl-4-phenylenediamine + NO2
oxidized tetrametyl-4-phenylenediamine + NO
-
no reaction with horse ferrocytochrome c, Neurospora europaea ferrocytochrome c-552, Magnetospirillum magnetotacticum ferrocytochrome c-550 and Pseudomonas aeruginosa cytochrome c-551
-
?
reduced tetramethyl-4-phenylenediamine + O2
oxidized tetrametyl-4-phenylenediamine + H2O
-
-
-
?
additional information
?
-
ferrocytochrome c + O2
ferricytochrome c + H2O
-
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
in the presence of ascorbate, N,N,N',N-tetramethyl-p-phenylenediamine and cytochrome c-553
-
?
ferrocytochrome c-551 + NO2-
NO + ferricytochrome c-551
-
-
-
?
ferrocytochrome c-551 + NO2-
NO + ferricytochrome c-551
-
-
-
?
ferrocytochrome c-551 + NO2-
NO + ferricytochrome c-551
-
-
-
?
ferrocytochrome c-551 + O2
ferricytochrome c-551 + H2O
-
-
-
?
ferrocytochrome c-551 + O2
ferricytochrome c-551 + H2O
-
-
-
-
?
ferrocytochrome c-551 + O2
ferricytochrome c-551 + H2O
-
-
-
?
ferrocytochrome c-551 + O2
H2O + ferricytochrome c-551
-
-
-
?
ferrocytochrome c-551 + O2
H2O + ferricytochrome c-551
-
-
-
?
ferrocytochrome c-551 + O2
H2O + ferricytochrome c-551
-
also reacts with horse heart cytochrome c
-
?
ferrocytochrome c-551 + O2
H2O + ferricytochrome c-551
-
-
-
?
ferrocytochrome c-551 + O2
H2O + ferricytochrome c-551
-
-
-
?
ferrocytochrome c-551 + O2
H2O + ferricytochrome c-551
-
-
-
-
?
ferrocytochrome c-551 + O2
H2O + ferricytochrome c-551
-
inactive with eukaryotic cytochromes c
-
?
nitric oxide + H2O + ferricytochrome c
nitrite + ferrocytochrome c + H+
-
-
-
-
r
nitric oxide + H2O + ferricytochrome c
nitrite + ferrocytochrome c + H+
-
-
-
-
r
nitric oxide + H2O + ferricytochrome c551
nitrite + ferrocytochrome c551 + H+
-
-
-
-
r
nitric oxide + H2O + ferricytochrome c551
nitrite + ferrocytochrome c551 + H+
-
-
-
r
nitrite + electron donor
NO + oxidized electron donor + H2O
-
mitochondrial electron carrier cytochrome c can also effectively reduce nitrite to NO. This nitrite reductase activity is highly regulated as it is dependent on pentacoordination of the heme iron in the protein and occurs under anoxic and acidic conditions. In the presence of nitrite, pentacoordinate cytochrome c generates bioavailable NO that is able to inhibit mitochondrial respiration
-
-
?
nitrite + electron donor
NO + oxidized electron donor + H2O
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
artificial electron donor: reduced benzyl viologen
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
artificial electron donors: reduced methyl viologen, phenazine methosulfate and to a lesser extend hydroquinone, highly purified enzyme has cytochrome c oxidase activity
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
artificial electron donor: reduced benzyl viologen
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
artificial electron donors: thionine, brilliant cresyl blue, methylene blue, 2,6-dichlorophenolindophenol or Pseudomonas stutzeri cytochrome c-552 and 558
-
?
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c2
NO + H2O + ferricytochrome c2
-
-
-
-
?
nitrite + ferrocytochrome c2
NO + H2O + ferricytochrome c2
-
there is likely an unidentified electron donor, in addition to c2 that transfers electrons to nitrite reductase
-
-
?
nitrite + ferrocytochrome c550
NO + oxidized ferricytochrome c550
-
-
-
-
?
nitrite + ferrocytochrome c550
NO + oxidized ferricytochrome c550
-
-
-
-
?
nitrite + H2O + reduced pseudoazurin
nitric oxide + H+ + pseudoazurin
reduction of pseudoazurin by ascorbate
-
-
?
nitrite + H2O + reduced pseudoazurin
nitric oxide + H+ + pseudoazurin
reduction of pseudoazurin by ascorbate
-
-
?
nitrite + reduced azurin
NO + H2O + oxidized azurin
-
-
-
-
?
nitrite + reduced azurin
NO + H2O + oxidized azurin
-
-
-
-
?
nitrite + reduced azurin I
NO + oxidized azurin I
-
-
-
-
?
nitrite + reduced azurin I
NO + oxidized azurin I
-
coordinate synthesis of azurin I and copper nitrite reductase in Alcaligenes xylosoxidans during denitrification
-
-
?
nitrite + reduced benzyl viologen
NO + H2O + oxidized benzyl viologen
-
-
-
-
?
nitrite + reduced benzyl viologen
NO + H2O + oxidized benzyl viologen
-
-
-
-
?
nitrite + reduced benzyl viologen
NO + H2O + oxidized benzyl viologen
-
-
-
-
?
nitrite + reduced benzyl viologen
NO + oxidized benzyl viologen
-
random sequential mechanism
-
-
?
nitrite + reduced benzyl viologen
NO + oxidized benzyl viologen
-
-
-
?
nitrite + reduced benzyl viologen
NO + oxidized benzyl viologen
-
-
-
?
nitrite + reduced benzyl viologen
NO + oxidized benzyl viologen
-
-
-
-
?
nitrite + reduced benzyl viologen + 2 H+
nitric oxide + H2O + oxidized benzyl viologen
-
-
-
?
nitrite + reduced benzyl viologen + 2 H+
nitric oxide + H2O + oxidized benzyl viologen
-
-
-
-
?
nitrite + reduced electron donor
NO + H2O + oxidized electron donor
-
-
-
-
?
nitrite + reduced electron donor
NO + H2O + oxidized electron donor
-
-
-
-
?
nitrite + reduced electron donor
NO + H2O + oxidized electron donor
-
-
-
?
nitrite + reduced electron donor
NO + H2O + oxidized electron donor
-
-
-
?
nitrite + reduced hydroquinone
nitric oxide + H2O + hydroquinone
-
-
-
?
nitrite + reduced hydroquinone
nitric oxide + H2O + hydroquinone
-
-
-
?
nitrite + reduced methyl viologen
NO + oxidized methyl viologen + H2O
-
-
-
-
?
nitrite + reduced methyl viologen
NO + oxidized methyl viologen + H2O
-
-
-
-
?
nitrite + reduced methyl viologen
NO + oxidized methyl viologen + H2O
-
-
-
?
nitrite + reduced methyl viologen
NO + oxidized methyl viologen + H2O
-
-
-
?
nitrite + reduced phenazine methosulfate
NO + oxidized phenazine methosulfate
-
-
-
?
nitrite + reduced phenazine methosulfate
NO + oxidized phenazine methosulfate
-
-
-
?
nitrite + reduced phenazine methosulfate
NO + oxidized phenazine methosulfate
-
-
-
?
nitrite + reduced phenazine methosulfate
NO + oxidized phenazine methosulfate
-
-
-
?
nitrite + reduced phenazine methosulfate
NO + oxidized phenazine methosulfate
-
-
-
?
nitrite + reduced phenazine methosulfate
NO + oxidized phenazine methosulfate
-
-
-
?
nitrite + reduced phenazine methosulfate
NO + oxidized phenazine methosulfate
-
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
the rate-determining step in the enzyme reaction sequence is not the intermolecular electron transfer process between pseudoazurin and AcNIR, but the reduction of substrate by AcNIR in the steady-state assay system
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
the rate-determining step in the enzyme reaction sequence is not the intermolecular electron transfer process between pseudoazurin and AcNIR, but the reduction of substrate by AcNIR in the steady-state assay system
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
-
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
pseudoazurin from Achromobacter cycloclastes
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
-
-
-
r
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
random sequential mechanism
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
-
-
-
r
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
-
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
cytochrome c550 and pseudoazurin are the alternative electron mediator proteins between the cytochrome bc1 and the cytochrome cd1 type nitrite reductase
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
-
-
-
?
nitrite + reduced pseudoazurin + H+
nitric oxide + oxidized pseudoazurin + H2O
-
-
-
-
r
nitrite + reduced pseudoazurin + H+
nitric oxide + oxidized pseudoazurin + H2O
-
-
-
-
r
NO2- + ferrocytochrome c
NO + ferricytochrome c
-
role in respiration
-
-
?
NO2- + ferrocytochrome c
NO + ferricytochrome c
-
probably most dominant activity in vivo
-
?
NO2- + reduced ascorbate
NO + oxidized ascorbate
-
physiological electron donor is not known, 7% activity if NADH is used as artificial electron donor
-
?
NO2- + reduced ascorbate
NO + oxidized ascorbate
-
-
-
?
NO2- + reduced pseudoazurin
NO + oxidized pseudoazurin
-
-
-
?
NO2- + reduced pseudoazurin
NO + oxidized pseudoazurin
-
unambiguously identified as physiological electron donor
-
?
O2 + ferrocytochrome c
H2O + ferricytochrome c
-
-
-
-
?
O2 + ferrocytochrome c
H2O + ferricytochrome c
-
-
-
-
?
reduced azurin + O2
oxidized azurin + H2O
-
putative physiological electron donor
-
-
?
reduced azurin + O2
oxidized azurin + H2O
-
not known whether azurin donates electrons in vivo in parallel or sequentially to cytochrome c551
-
?
additional information
?
-
-
theoretical investigation has provided a number of insights into the reaction mechanism of copper nitrite reductase: The results presented in this paper indicate that the hydroxyl-intermediate pathway appears unlikely for the main reaction. The results also indicate that Asp-92 may play a significant structural role through hydrogen-bonding to the protonated oxygen of the nitrite substrate, and thereby elongating the N O bond, which is to be cleaved
-
-
?
additional information
?
-
density functional theory study of nitrite and nitric oxide adducts
-
-
?
additional information
?
-
the active site residue is Ile257. The small molecules formate, acetate and nitrate mimic the substrate by having at least two oxygen atoms for bidentate coordination to the type 2 copper atom and interacting wit the oxidized catalytic metal ion, overview. Nitrite and the substrate mimic bind in the same asymmetric, bidentate manner
-
-
?
additional information
?
-
the active site residue is Ile257. The small molecules formate, acetate and nitrate mimic the substrate by having at least two oxygen atoms for bidentate coordination to the type 2 copper atom and interacting wit the oxidized catalytic metal ion, overview. Nitrite and the substrate mimic bind in the same asymmetric, bidentate manner
-
-
?
additional information
?
-
-
the active site residue is Ile257. The small molecules formate, acetate and nitrate mimic the substrate by having at least two oxygen atoms for bidentate coordination to the type 2 copper atom and interacting wit the oxidized catalytic metal ion, overview. Nitrite and the substrate mimic bind in the same asymmetric, bidentate manner
-
-
?
additional information
?
-
-
cross-linked hemoglobin bis-tetramers with good oxygen delivery potential have 3fold enhanced nitrite reductase activity, compared to native protein and cross-linked tetramers. Conjugation of four polyethylene glocol chains to the bis-tetramer at each beta-Cys-93 produces a material with additionallly 2.5fold increased nitrite reductase activity while retaining cooperativity
-
-
?
additional information
?
-
mARC can generate nitric oxide from nitrite when forming an electron transfer chain with NADH, cytochrome b5, and NADH-dependent cytochrome b5 reductase
-
-
?
additional information
?
-
mARC can generate nitric oxide from nitrite when forming an electron transfer chain with NADH, cytochrome b5, and NADH-dependent cytochrome b5 reductase
-
-
?
additional information
?
-
-
mARC can generate nitric oxide from nitrite when forming an electron transfer chain with NADH, cytochrome b5, and NADH-dependent cytochrome b5 reductase
-
-
?
additional information
?
-
a conserved and functional aniA gene is not essential for meningococcal survival
-
-
?
additional information
?
-
-
enzyme catalyzes the reduction of NO2- to NO, the oxidation of hydroxylamine (NH2OH) to NO, reaction of EC 1.7.2.6, and the production of N2O from NH2OH and NO2
-
-
-
additional information
?
-
enzyme catalyzes the reduction of NO2- to NO, the oxidation of hydroxylamine (NH2OH) to NO, reaction of EC 1.7.2.6, and the production of N2O from NH2OH and NO2
-
-
-
additional information
?
-
enzyme catalyzes the reduction of NO2- to NO, the oxidation of hydroxylamine (NH2OH) to NO, reaction of EC 1.7.2.6, and the production of N2O from NH2OH and NO2
-
-
-
additional information
?
-
-
simulation of the NO kinetics observed in batch cultures of Paracoccus denitrificans, including aerobic and anaerobic growth, the kinetics of O2 consumption and denitrification. The model predicts NO concentrations close to that measured. The predicted steady-state NO aqueous concentration for an actively denitrifying population is 35 nM
-
-
?
additional information
?
-
activity is associated with histidine/methionine coordination at heme c, and the cytochrome cd1 is activated by exposure to its physiological substrate without the necessity of passing through the reduced state
-
-
?
additional information
?
-
-
activity is associated with histidine/methionine coordination at heme c, and the cytochrome cd1 is activated by exposure to its physiological substrate without the necessity of passing through the reduced state
-
-
?
additional information
?
-
-
nitrite reductase from Pseudomonas aeruginosa released by antimicrobial agents and complement induces interleukin-8 production in bronchial epithelial cells
-
-
?
additional information
?
-
-
nitrite reductase in both oxidized and reduced states forms with NO two distinct compounds at both hemes. These compounds, in addition to the oxidized and reduced enzymes, are formed during the turnover of this enzyme as functional intermediates
-
-
?
additional information
?
-
-
spectroscopic analysis of the reactivity of cd1NiR and its semi-apo derivative with NO. The c heme nitrosylation is enhanced during catalysis
-
-
?
additional information
?
-
-
nitrite reductase from Pseudomonas aeruginosa released by antimicrobial agents and complement induces interleukin-8 production in bronchial epithelial cells
-
-
?
additional information
?
-
activity is associated with histidine/methionine coordination at heme c, and the cytochrome cd1 is activated by exposure to its physiological substrate without the necessity of passing through the reduced state, reactivity toward nitrite is also observed for oxidized cytochrome cd1 from Pseudomonas stutzeri suggesting a more general involvement of the EPR-silent FeIII heme d1 species in nitrite reduction
-
-
?
additional information
?
-
-
activity is associated with histidine/methionine coordination at heme c, and the cytochrome cd1 is activated by exposure to its physiological substrate without the necessity of passing through the reduced state, reactivity toward nitrite is also observed for oxidized cytochrome cd1 from Pseudomonas stutzeri suggesting a more general involvement of the EPR-silent FeIII heme d1 species in nitrite reduction
-
-
?
additional information
?
-
activity is associated with histidine/methionine coordination at heme c, and the cytochrome cd1 is activated by exposure to its physiological substrate without the necessity of passing through the reduced state, reactivity toward nitrite is also observed for oxidized cytochrome cd1 from Pseudomonas stutzeri suggesting a more general involvement of the EPR-silent FeIII heme d1 species in nitrite reduction
-
-
?
additional information
?
-
-
electrocatalytic reduction of nitrite to NO by CuMe2bpaCl2, as a model for the active site of copper containing nitrite reductase. The 77-K EPR spectrum of CuMe2bpaCl2 in the collagen matrix reveals the typical axial signals of a tetragonal Cu2+ chromophore. The redox potential is -63 mV at pH 5.5. In the presence of nitrite, an increase in the cathodic current is observed in the cyclic voltammogram of CuMe2bpaCl2 in the collagen matrix. Upon reaching -300 mV, a linear generation of NO is observed for the CuMe2bpaCl2/collagen film-coated electrode. The relationship between the rate of NO generation and the nitrite concentration in solution using the Michaelis-Menten equation, results in Vmax 3.16 nM per s and Km 1.1 mM at pH 5.5. The current increase and the reaction rate are dependent on the pH of the solution. The mechanism of nitrite reduction by the copper complex in the collagen matrix is the same mechanism as that of the enzyme in aqueous solution
-
-
?
additional information
?
-
-
study on structure-function relationship using copper(I)-nitrite complexes with sterically hindered tris(4-imidazolyl)carbinols such as tris(1-methyl-2-ethyl-4-imidazolyl)carbinol, tris(1-methyl-2-isopropyl-4-imidazolyl)carbinol, or tris(1-pyrazolyl)methanes such as tris(3,5-dimethyl-1-pyrazolyl)methane or tris(3,5-diethyl-1-pyrazolyl)methane, and tris(3,5-diisopropyl-1-pyrazolyl)methane. All of these complexes are good functional models of Cu-NiR that form NO and copper(II) acetate complexes well from reactions with acetic acid under anaerobic conditions. The copper(I) nitrite complex with the tris(1-methyl-2-ethyl-4-imidazolyl)carbinol ligand, which is similar to the highly conserved three-histidine (His)3 ligand environment in the catalytic site of Cu-NiR, has the highest Cu-NiR activity
-
-
?
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ferrocytochrome c-551 + O2
ferricytochrome c-551 + H2O
-
-
-
?
nitric oxide + H2O + ferricytochrome c552
nitrite + ferrocytochrome c552 + 2 H+
Marinobacter nauticus
-
-
-
-
?
nitrite + electron donor
NO + oxidized electron donor
-
-
-
-
?
nitrite + electron donor
NO + oxidized electron donor + H2O
-
mitochondrial electron carrier cytochrome c can also effectively reduce nitrite to NO. This nitrite reductase activity is highly regulated as it is dependent on pentacoordination of the heme iron in the protein and occurs under anoxic and acidic conditions. In the presence of nitrite, pentacoordinate cytochrome c generates bioavailable NO that is able to inhibit mitochondrial respiration
-
-
?
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
nitrite + ferrocytochrome c2
NO + H2O + ferricytochrome c2
-
there is likely an unidentified electron donor, in addition to c2 that transfers electrons to nitrite reductase
-
-
?
nitrite + ferrocytochrome c550
NO + ferricytochrome c550
-
-
-
-
?
nitrite + reduced azurin I
NO + oxidized azurin I
-
coordinate synthesis of azurin I and copper nitrite reductase in Alcaligenes xylosoxidans during denitrification
-
-
?
nitrite + reduced electron donor
NO + H2O + oxidized electron donor
nitrite + reduced pseudoazurin
NO + H2O + oxidized pseudoazurin
-
-
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
NO2- + ferrocytochrome c
NO + ferricytochrome c
NO2- + reduced cytochrome c550
NO + oxidized cytochrome c550
-
unambiguously identified as physiological electron donor
-
?
NO2- + reduced pseudoazurin
NO + oxidized pseudoazurin
-
unambiguously identified as physiological electron donor
-
?
reduced azurin + O2
oxidized azurin + H2O
additional information
?
-
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + reduced electron donor
NO + H2O + oxidized electron donor
-
-
-
-
?
nitrite + reduced electron donor
NO + H2O + oxidized electron donor
-
-
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
-
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
-
-
-
r
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
-
-
-
r
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
cytochrome c550 and pseudoazurin are the alternative electron mediator proteins between the cytochrome bc1 and the cytochrome cd1 type nitrite reductase
-
-
?
NO2- + ferrocytochrome c
NO + ferricytochrome c
-
role in respiration
-
-
?
NO2- + ferrocytochrome c
NO + ferricytochrome c
-
probably most dominant activity in vivo
-
?
reduced azurin + O2
oxidized azurin + H2O
-
putative physiological electron donor
-
-
?
reduced azurin + O2
oxidized azurin + H2O
-
not known whether azurin donates electrons in vivo in parallel or sequentially to cytochrome c551
-
?
additional information
?
-
-
cross-linked hemoglobin bis-tetramers with good oxygen delivery potential have 3fold enhanced nitrite reductase activity, compared to native protein and cross-linked tetramers. Conjugation of four polyethylene glocol chains to the bis-tetramer at each beta-Cys-93 produces a material with additionallly 2.5fold increased nitrite reductase activity while retaining cooperativity
-
-
?
additional information
?
-
a conserved and functional aniA gene is not essential for meningococcal survival
-
-
?
additional information
?
-
-
nitrite reductase from Pseudomonas aeruginosa released by antimicrobial agents and complement induces interleukin-8 production in bronchial epithelial cells
-
-
?
additional information
?
-
-
nitrite reductase from Pseudomonas aeruginosa released by antimicrobial agents and complement induces interleukin-8 production in bronchial epithelial cells
-
-
?
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1.33
ferricytochrome c
-
succinylated monomeric enzyme
1.9
ferricytochrome c B0428
pH 5.5, 25°C
-
0.583 - 796
ferricytochrome c551
-
0.025 - 0.043
Ferrocytochrome c-551
-
0.1
ferrocytochrome V(gamma)
-
-
-
7
reduced ascorbate
-
25°C, pH 6.9, recombinant enzyme
additional information
additional information
-
-
-
1
azurin
-
recombinant Y10F mutant enzyme, at pH 6.2 and 27°C
1.12
azurin
-
recombinant wild-type enzyme, at pH 6.2 and 27°C
0.583
ferricytochrome c551
-
recombinant wild-type enzyme, at pH 6.2 and 27°C
-
0.6
ferricytochrome c551
-
recombinant Y10F mutant enzyme, at pH 6.2 and 27°C
-
2.8
ferricytochrome c551
-
at pH 7.0
-
796
ferricytochrome c551
pH 8.0, 25°C
-
0.025
Ferrocytochrome c-551
pH 6.2, 25°C, wild-type enzyme
-
0.032
Ferrocytochrome c-551
pH 6.2, 25°C, mutant enzyme H369A
-
0.043
Ferrocytochrome c-551
pH 6.2, 25°C, mutant enzyme H327A
-
0.08
hydroxylamine
-
25°C, pH 7.0, electron donor cytochrome c550
0.2
hydroxylamine
-
25°C, pH 7.0, electron donor horse heart cytochrome c
3
hydroxylamine
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor horse heart cytochrome c
3.2
hydroxylamine
-
25°C, pH 7.0, wild-type, pre-reduction with dithionite
3.5
hydroxylamine
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor cytochrome c550
6.4
hydroxylamine
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor pseudoazurin
7.7
hydroxylamine
-
25°C, pH 7.0, Y25S mutant enzyme
0.08
NH2OH
-
initially oxidized enzyme, electron donor cytochrome c550
0.2
NH2OH
-
initially oxidized enzyme, electron donor horse heart cytochrome c
3
NH2OH
-
pre-reduced enzyme, electron donor horse heart cytochrome c
3.5
NH2OH
-
pre-reduced enzyme, electron donor cytochrome c550
6.4
NH2OH
-
pre-reduced enzyme, electron donor pseudoazurin
0.08
nitrite
pH 6.2, 25°C, mutant enzyme H327A
0.08
nitrite
pH 6.2, 25°C, mutant enzyme H369A
0.1
nitrite
pH 7.4, temperature not specified in the publication
0.62
nitrite
-
pH 7.0, electron donor azurin
1.1
nitrite
wild-type, pH 6.5, 25°C
2.1
nitrite
-
25°C, pH 7.0, electron donor cytochrome c550
2.3
nitrite
core protein, pH 6.5, 25°C
2.4
nitrite
-
25°C, pH 7.0, electron donor horse heart cytochrome c
2.6
nitrite
core protein carrying mutation Y327F, pH 6.5, 25°C
2.7
nitrite
-
25°C, pH 7.0, wild-type, without pre-reduction with dithionite
3.1
nitrite
at pH 8.0 and 25°C
5.3
nitrite
-
25°C, pH 7.0, electron donor pseudoazurin
8
nitrite
pH 6.2, 25°C, wild-type enzyme
41
nitrite
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor horse heart cytochrome c
67
nitrite
-
25°C, pH 7.0, Y25S mutant enzyme
68
nitrite
-
25°C, pH 7.0, wild-type, pre-reduction with dithionite
71
nitrite
-
25°C, pH 8.0
74
nitrite
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor cytochrome c550
144
nitrite
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor pseudoazurin
219
nitrite
-
25°C, pH 7.5
243
nitrite
-
pH 7.0, electron donor benzyl viologen
320
nitrite
-
25°C, pH 5.5
392
nitrite
-
25°C, pH 7.0
1046
nitrite
-
25°C, pH 6.5
1478
nitrite
-
25°C, pH 6.0
38
NO
-
25°C, pH 6.5
0.08
NO2-
recombinant H327A and H369a mutant enzymes
2.1
NO2-
-
initially oxidized enzyme, electron donor cytochrome c550
2.4
NO2-
-
initially oxidized enzyme, electron donor horse heart cytochrome c
5.3
NO2-
-
initially oxidized enzyme, electron donor pseudoazurin
8
NO2-
recombinant wild-type enzyme
41
NO2-
-
pre-reduced enzyme, electron donor horse heart cytochrome c
74
NO2-
-
pre-reduced enzyme, electron donor cytochrome c550
80
NO2-
-
electron donor: reduced tetramethyl-4-phenylenediamine
106
NO2-
-
all-ferric nitrite-bound complex, electron donor pseudoazurin
144
NO2-
-
pre-reduced enzyme, electron donor pseudoazurin
0.11
O2
-
initially oxidized enzyme, electron donor horse heart cytochrome c
0.11
O2
-
25°C, pH 7.0, electron donor horse heart cytochrome c
0.17
O2
-
initially oxidized enzyme, electron donor cytochrome c550
0.17
O2
-
25°C, pH 7.0, electron donor cytochrome c550
2.8
O2
-
pre-reduced enzyme, electron donor horse heart cytochrome c
2.8
O2
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor horse heart cytochrome c
3
O2
-
pre-reduced enzyme, electron donor cytochrome c550
3
O2
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor cytochrome c550
3.2
O2
-
25°C, pH 7.0, wild-type, pre-reduction with dithionite
6.2
O2
-
25°C, pH 7.0, Y25S mutant enzyme
6.4
O2
-
pre-reduced enzyme, electron donor pseudoazurin
6.4
O2
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor pseudoazurin
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evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
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the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
-
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
-
evolution
-
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
-
evolution
-
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
-
evolution
-
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
-
evolution
-
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
-
evolution
-
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
-
evolution
-
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
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metabolism
the enzyme catalyzes the key reaction in denitrification as the nitrogen compound is changed from an ionic state to a gaseous molecule
metabolism
the enzyme is involved in the denitrification anoxic process, which occurs in four reduction steps: initial conversion of nitrate to nitrite, followed by transformation of nitrite to nitric oxide, subsequent reduction of nitric oxide to nitrous oxide, and the final conversion of nitrous oxide to dinitrogen gas. All stages are catalyzed by complex metalloenzymes with different transition metal cofactors. Dissimilatory nitrite reductases (NiRs) catalyze the reduction of nitrite to nitric oxide, the committed step in denitrification. There are two main types: one containing iron (cd1NiRs) and the other copper (CuNiRs)
metabolism
4-domain variant of enzyme utilizes N-terminal tethering for downregulating enzymatic activity. Tethering communicates the redox state of the heme to the distant type 2 copper center that helps initiate substrate binding for catalysis
metabolism
tethering does not enhance the rate of electron delivery from its pendant cytochrome c to the catalytic copper-containing core. Tethering communicates the redox state of the heme to the distant type 2 copper center that helps initiate substrate binding for catalysis. It also tunes copper reduction potentials, suppresses reductive enzyme inactivation, enhances enzyme affinity for substrate, and promotes inter-copper electron transfer. Nitrite binding and enzyme turnover is controlled by heme reduction and prevents NiR inactivation
metabolism
the driving force for electron transfer from type 1 copper to type 2 copper comes from a remote water-mediated triple-proton-coupled electron-transfer mechanism. In the high-pH proton channel, the water-mediated triple-proton transfer occurs from Glu113 to an intermediate water molecule, whereas in the primary channel, the transfer is from Lys128 to His260. Subsequently, the two channels employ another two or three distinct proton-transfer steps to deliver the proton to the nitrite substrate at the type 2 copper site
metabolism
-
tethering does not enhance the rate of electron delivery from its pendant cytochrome c to the catalytic copper-containing core. Tethering communicates the redox state of the heme to the distant type 2 copper center that helps initiate substrate binding for catalysis. It also tunes copper reduction potentials, suppresses reductive enzyme inactivation, enhances enzyme affinity for substrate, and promotes inter-copper electron transfer. Nitrite binding and enzyme turnover is controlled by heme reduction and prevents NiR inactivation
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metabolism
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the enzyme catalyzes the key reaction in denitrification as the nitrogen compound is changed from an ionic state to a gaseous molecule
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physiological function
deletion of cytochrome cd1-type nitrite reductase NirS gene or gene NirN results in impaired growth and smaller, fewer, and aberrantly shaped magnetite crystals during nitrate reduction. Nitrite reduction is completely abolished in the DELTAnirS mutant. NirN is required for full reductase activity of NirS by maintaining a proper form of d1 heme for holo-cytochrome cd1 assembly
physiological function
copper-containing nitrite reductase (CuNIR) catalyzes the reduction of nitrite (NO2 ) to nitric oxide (NO) during denitrification
physiological function
dissimilatory reduction of nitrite by copper-containing nitrite reductase (CuNiR) is an important step in the geobiochemical nitrogen cycle
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
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Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
purified recombinant MRA2164 protein shows significant nitrite dependent NO synthesizing activity. The knockdown of the MRA2164 gene expression results in a significantly reduced NO level compared to the wild type bacilli with a simultaneous return of its replicative capability
physiological function
strain has two copies of nirK, a 4-domain NiR. and a 2-domain NiR, referred to for clarity as 2DNiR. 2dNir shows anbout 5% of the activtiy of the 4-domain variant
physiological function
under denitrifying conditions, the copper-containing nitrite reductase NirK and cytochrome cd1 nitrite reductase NirS single deletion mutants grow normally and their nitrite reductase activity is not affected. The NirKS double mutant grows more slowly. The NirS gene product, but not that of NirK, maintains swimming motility of strain S58 under aerobic and low-oxygen conditions in the presence of nitrate
physiological function
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Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
-
physiological function
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under denitrifying conditions, the copper-containing nitrite reductase NirK and cytochrome cd1 nitrite reductase NirS single deletion mutants grow normally and their nitrite reductase activity is not affected. The NirKS double mutant grows more slowly. The NirS gene product, but not that of NirK, maintains swimming motility of strain S58 under aerobic and low-oxygen conditions in the presence of nitrate
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physiological function
-
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
-
physiological function
-
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
-
physiological function
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purified recombinant MRA2164 protein shows significant nitrite dependent NO synthesizing activity. The knockdown of the MRA2164 gene expression results in a significantly reduced NO level compared to the wild type bacilli with a simultaneous return of its replicative capability
-
physiological function
-
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
-
physiological function
-
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
-
physiological function
-
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
-
physiological function
-
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
-
physiological function
-
dissimilatory reduction of nitrite by copper-containing nitrite reductase (CuNiR) is an important step in the geobiochemical nitrogen cycle
-
physiological function
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copper-containing nitrite reductase (CuNIR) catalyzes the reduction of nitrite (NO2 ) to nitric oxide (NO) during denitrification
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additional information
determination of the activation energies, transition states, and minimum energy pathways of CuNiR for reaction mechanism analysis. Structure modelling of the CuNiR active site involving residues His100, His135, His306, Asp98, His255, Ile257 and four water molecules. Structure-function analysis, detailed overview
additional information
geometric structure of the nitrite-bound T2 Cu site in GtNiR using density functional theory, DFT, calculations. The reduction of T2 Cu site promotes the proton transfer. Optimized structures of nitrite binding forms under physiological pH conditions and in neutral states, detailed overview
additional information
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geometric structure of the nitrite-bound T2 Cu site in GtNiR using density functional theory, DFT, calculations. The reduction of T2 Cu site promotes the proton transfer. Optimized structures of nitrite binding forms under physiological pH conditions and in neutral states, detailed overview
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atomic resolution structures of four forms of the green Cu-nitrite reductase: structure of the resting state of the enzyme at 0.9 A, structure of then nitrite-soaked complex at 1.10 A resolution, structure of the endogenously bound NO complex at 1.12-A resolution, structure of endogenously bound nitrite and NO in the same crystal at 1.15-A resolution
mutant H254F loaded with either Cu2+ or Zn2+, to 1.5 A and 1.85 A, respectively. Both structures are essentially identical. Structure of mutant N90S, to 1.6 A resolution. In both the native and mutant N90S structures, a surface Zn ion is present in each monomer, bridging the two monomers through the coordinating residues His165 and Asp167 of one monomer and Glu195 of the adjacent monomer. This Zn site is similar to that described previously in several NiR structures
sitting-drop vapour diffusion method. Crystal structures of M144L and M144Q at 1.9 A, crystal structure of native enzyme at 1.04 A, structure of mutant enzyme C130A at 1.35 A
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use of crystallography, together with online X-ray absorption spectroscopy and optical spectroscopy, to show that X-rays rapidly and selectively photoreduce the type 1 Cu centre, but that the type 2 Cu centre does not photoreduce directly over a typical crystallographic data collection time. Internal electron transfer between the type 1 Cu and type 2 Cu centres does not occur, and the type 2 Cu centre remains oxidized
crystals are grown at 19°C by hanging drop vapour diffusion using a reservoir of 100 mM sodium acetate, pH 4.7, 6%-10% polyethylene glycol 4000 and 1-5 mM cupric chloride, each drop is made from an equal volume of reservoir and a 15 mg/ml protein stock solution buffered in 10 mM Tris pH 7.0, crystals of mutants diffract to 1.8 A, nitrite-soaked oxidized crystals are obtained by placing crystals in reservoir solution supplemented with 5 mM sodium nitrite
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hanging-drop vapor-diffusion method, mutant enzyme M150G
M150G crystals are grown at room temperature by hanging drop vapor diffusion method
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purified recombinant enzyme, free or in complex with small molecule inhibitors, hanging drop vapor diffusion method, room temperature, 25 mg/ml protein in 20 mM Tris-HCl, pH 7.0, is mixed with an equal volume of reservoir containing 6-10% PEG 4000, 100 mM sodium acetate, pH 4.0, addition of 20 mM of ligands 20 mM of azide, formate, or nitrate, X-ray diffraction structure determination and analysis at 1.5-1.8 A resolution
recombinant soluble domain, residues 483-913, to 2.4 A
structures of copper-containing nitrite reductase NiR and the N-terminal 68 residue-deleted mutant, at resolutions of 1.3 A and 1.8 A, respectively. Both structures show a striking resemblance with the overall structure of the well-known copper-containing nitrite reductases composed of two Greek key beta-barrel domains. The N-terminal region has one beta-strand and one alpha-helix extended to the northern surface of the type-1 copper site. This region contributes to the transient binding with the partner protein during the interprotein electron transfer reaction in the Geobacillus system. The region is directly involved in the specific partner recognition
crystal structure analysis and computational modelling, the model includes the T2 Cu site, the nitrite, three His residues coordinated to the T2 Cu site, and the second sphere residues Asp98, His244, and Val246. Additionally, two water molecules are included. One water molecule is labeled WAT1 occupying an intermediate position between Asp98 and His244 and another is labeled WAT2 and seems to interact with Asp98 in the initial coordinates of the X-ray structure, from PDB ID 3WKP
purified wild-type enzyme with chloride- and formate-bound, as well as purified enzyme mutant C135A with nitrite-bound, hanging drop vapour diffusion method, mixng of 0.0015 ml of 100 mg/ml protein solution with 0.001 5 ml of well solution containing 0.1 M acetate buffer, pH 4.5, 5.0% w/v PEG 4000, 75 mM CuSO4, and 200 mM sodium formate, and equilibration against 0.45 ml well solution, soaking of C135A mutant crystals in nitrite solution, at 20°C, X-ray diffraction structure determination and analysis at 1.15 A and 1.90 A resolution, respectively
the dioxygen present in an aerobically manipulated crystal can bind to the catalytic type 2 copper site of NirK during anaerobic synchrotron-radiation crystallography experiments. The structure shows a dual conformation of one water molecule as an axial ligand in the type 2 copper site. In the structure of the C135A mutant with peroxide bound to the type 2 copper atom, the peroxide molecule is mainly observed in a side-on binding manner, with a possible minor end-on conformation
hanging drop vapour diffusion, 0.002 ml protein solution containing 20 mg/ml protein in 20 mM Tris-Hcl, pH 7.5 are mixed with reservoir solution containing 18% polyethylene glycol 4000 and 100 mM Tris-HCl, pH 8.9 at 20°C, crystals of wild-type HdNIR and C260A mutant diffract to 2.35 A and 3.5 A, respectively
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in complex with its electron-donor protein pseudoazurin
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the type 1 copper in the N-terminal tethered cupredoxin domain is placed too far away from the catalytic core type i copper for effective electron transfer. The N-terminal peptide that carries His27 plays a role in water-mediated anchoring of the substrate at the type 2 copper site
molecular docking simulations with cytochrome c552 or cytochrome c show that hydrophobic interactions favor the formation of complexes where the heme c domain of the enzyme is the principal docking site. Only for cytochrome c552 the preferential areas of contact and Fe-Fe distances between heme groups of the redox partners allow establishing competent electron transfer pathways. The coupling of the enzyme with chemical redox mediators is not energetically favorable
Marinobacter nauticus
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crystals of Y25S mutant protein are grown from a solution containing 10-20 mg/ml protein in the presence of 2.2-2.4 M ammonium sulfate and 50 mM potassium phosphate, pH 7.0, crystals diffract to 1.4 A
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molecular modeling of myglobin mutant L29H/F43Y with or without nitrite shows the necessary structural features of native cytochrome cd1 nitrite reductase and that the protein can provide comparable interactions with nitrite as in native nitrite reductase
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to 1.95 A resolution. The naturally fused type of Cu-nitrite reductase tethering a cytochrome c at the C-terminus folds as a unique trimeric domain-swapped structure and has a self-sufficient electron flow system. The C-terminal cytochrome c domain is located at the surface of the type 1 copper site in the N-terminal domain from the adjacent subunit. The heme-to-Cu distance of 10.6 A is comparable to the transient electron transfer complex of normal Cu-nitrite reductase with cytochrome c. The cytochrome c-Cu-nitrite reductase domain interaction is highly transient. An electron is directly transferred from the partner to the type 1 copper
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crystals of the H327A mutant are obtained by vapor diffusion technique by mixing in a 1:1 ratio the protein and a reservoir solution containing 4.0% polyethylene glycol 5000 monomethyl ether, 0.1 M sodium acetate, pH 5.5. The space group is 4(3)22 with cell dimensions 70.5 x 70.5 x 281 A. Crystals of the H369A mutant are obtained by mixing in a 1.1 ratio the protein and a reservoir solution containing 11.5% polyethylene glycol 6000, 0.2 M imidazole/malate, pH 6.5. The space group is P4(1)2(1)2 with cell dimensions 94.7 x 94.7 x 159.9 A
crystals of the H327A mutants are obtained by vapour diffusion technique. Crystals of H369A are obtained by mixing equal volumes of a reservoir solution containing 11.5% PEG 6000, 0.2 M imidazole/malate, pH 6.5, and of protein, in presence or not of 50 mM potassium nitrite and 50 mM sodium ascorbate. Crystals belong to space group P4(1)2(1)2 with cell dimensions a = b = 94.7 A, c = 159.9 A. The three-dimensional structures of NIR mutant H327A, and H369A in complex with NO solved by multiple wave-length anomalous dispersion, using the iron anomalous signal, and molecular replacement techniques. In both refined crystal structures the c-heme domain, whilst preserving its classical c-type cytochrome fold, has undergone a 60° rigid-body rotation around an axis parallel with the pseudo 8-fold axis of the beta-propeller, and passing through residue Gln115. Even though the distance between the Fe ions of the c and d1-heme remains 21 A, the edge-to-edge distance between the two hemes has increased by 5 A. Furthermore the distal side of the d1-heme pocket appears to have undergone structural re-arrangement and Tyr10 has moved out of the active site. In the H369A-NO complex, the position and orientation of NO is significantly different from that of the NO bound to the reduced wild-type structure
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H327A mutant enzymes: vapour diffusion technique, mixing of the enzyme and a reservoir solution containing 4% polyethylene glycol 5000 monomethyl ether, 100 mM sodium acetate pH 5.5 in a 1/1 ratio, H369A mutant enzyme: 11.5% polyethylene glycol 6000, 200 mM imidazole/malate pH 6.5, x-ray structure of both mutants
structure of the reduced enzyme both in the unbound form and with the physiological product, NO, bound at the d1 heme active site
the structure of the orthorhombic form (P2(1)2(1)2) of oxidized NiR-Pa is solved at 2.15 A resolution, using molecular replacement with the coordinates of the NiR from Thiosphaera pantotropha as the starting model
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vapour diffusion at 20°C, in presence of 10% polyethylene glycol 4000, 50 mM Tris-HCl, pH 8.7, 400 mM NaCl, at a protein concentration of 14 mg/ml. The crystals are dark green elongated tetragonal prisms of dimensions 1.5 mm * 0.2 mm * 0.2 mm for the largest ones. These crystals are tetragonal with space group P4(1)(3)2(1)2 and cell dimensions a = b = 128.2 A, c = 172.6 A. They diffract at least up to 2.8 A
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structures of copper(I)-nitrite complexes with sterically hindered tris(4-imidazolyl)carbinols such as tris(1-methyl-2-ethyl-4-imidazolyl)carbinol, tris(1-methyl-2-isopropyl-4-imidazolyl)carbinol, or tris(1-pyrazolyl)methanes such as tris(3,5-dimethyl-1-pyrazolyl)methane or tris(3,5-diethyl-1-pyrazolyl)methane, and tris(3,5-diisopropyl-1-pyrazolyl)methane reveal mononoclear ny1-N-bound nitrite complexes with a distorted tetrahedral geometry
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homology modeling based on PDB entry 1BKW. Model demonstrates that the enzyme can be folded into two cupredoxin domains of the well-known CuNIR structure and implies that the conserved residues H122, D125, H127, H158, C159, H168, M173,H272, and H321 form the type 1 and type 2 Cu sites
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W144L
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visible absorption and EPR spectrum is similar to that of wild-type AcNIR. The redox potentials of the mutant is also nearly equal to that of wild-type. Although the enzymatic activities of the mutants are also the same as that of wild-type enzyme, the intermolecular electron transfer rate constants from pseudoazurin to mutant AcNIRs is 3-4fold less than that from pseudoazurin to wild-type AcNIR using electrochemical methods
W144L/Y203L
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visible absorption and EPR spectrum is similar to that of wild-type AcNIR. The redox potentials of the mutant is also nearly equal to that of wild-type. Although the enzymatic activities of the mutants are also the same as that of wild-type enzyme, the intermolecular electron transfer rate constants from pseudoazurin to mutant AcNIRs is 3-4fold less than that from pseudoazurin to wild-type AcNIR using electrochemical methods
Y203L
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visible absorption and EPR spectrum is similar to that of wild-type AcNIR. The redox potentials of the mutant is also nearly equal to that of wild-type. Although the enzymatic activities of the mutants are also the same as that of wild-type enzyme, the intermolecular electron transfer rate constants from pseudoazurin to mutant AcNIRs is 3-4fold less than that from pseudoazurin to wild-type AcNIR using electrochemical methods
W144L
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visible absorption and EPR spectrum is similar to that of wild-type AcNIR. The redox potentials of the mutant is also nearly equal to that of wild-type. Although the enzymatic activities of the mutants are also the same as that of wild-type enzyme, the intermolecular electron transfer rate constants from pseudoazurin to mutant AcNIRs is 3-4fold less than that from pseudoazurin to wild-type AcNIR using electrochemical methods
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W144L/Y203L
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visible absorption and EPR spectrum is similar to that of wild-type AcNIR. The redox potentials of the mutant is also nearly equal to that of wild-type. Although the enzymatic activities of the mutants are also the same as that of wild-type enzyme, the intermolecular electron transfer rate constants from pseudoazurin to mutant AcNIRs is 3-4fold less than that from pseudoazurin to wild-type AcNIR using electrochemical methods
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Y203L
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visible absorption and EPR spectrum is similar to that of wild-type AcNIR. The redox potentials of the mutant is also nearly equal to that of wild-type. Although the enzymatic activities of the mutants are also the same as that of wild-type enzyme, the intermolecular electron transfer rate constants from pseudoazurin to mutant AcNIRs is 3-4fold less than that from pseudoazurin to wild-type AcNIR using electrochemical methods
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A191E
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slight increase in electron transfer rate constant
A191E/G198E
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3fold increase in electron transfer rate constant
A83D
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slight increase in electron transfer rate constant
A83D/A191E
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3fold increase in electron transfer rate constant
A83D/A191E/G198E
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4.7fold increase in electron transfer rate constant
A83D/G198E
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3fold increase in electron transfer rate constant
C130A
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inactive mutant enzyme, the loss of activity in this mutant is due to the absence of T1Cu and loss of the CuCys130Sg bond rather than any change to the protein structure in this region
D92E
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mutation in type 2 Cu center, very low activity with artificial electron donors methyl viologen and sodium dithionite, 20-30% of wild-type activity with physiological electron donor azurin I
D92N
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mutation in type 2 Cu center, very low activity with artificial electron donors methyl viologen and sodium dithionite, 60-70% of wild-type activity with physiological electron donor azurin I
G198E
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2.6fold increase in electron transfer rate constant
H139A
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mutation in type 1 Cu center, very low activity with the artificial electron donor methyl viologen, no activity with the physiological electron donor azurin I
H254F
full catalytic activity despite disruption of the primary proton channel. No change in apparent Km value for nitrite
M144L
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change in activity in the mutant is related to the perturbation of the finely poised redox potentials of the T1Cu sites of azurin and AxNiR
M144Q
-
change in activity in the mutant is related to the perturbation of the finely poised redox potentials of the T1Cu sites of azurin and AxNiR
N90S
disruption of H-bonding in the high-pH proton channel results in an 70% decrease in specific activity. No change in apparent Km value for nitrite
I257A
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3.7% of wild-type activity
I257G
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2.5% of wild-type activity
I257L
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26% of wild-type activity
I257M
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4% of wild-type activity
I257T
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1.4% of wild-type activity
I257V
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125% of wild-type activity
M150H
mutant enzyme shows very low catalytic activity
I257A
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3.7% of wild-type activity
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I257G
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2.5% of wild-type activity
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I257L
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26% of wild-type activity
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I257M
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4% of wild-type activity
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I257V
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125% of wild-type activity
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M150H
-
mutant enzyme shows very low catalytic activity
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D439N
about 7% of wild-type activity
C43S
mutation leads to disruption of a disulfide bridge. Mutant is a trimer in solution and shows similar spectroscopic properties and enzymatic activity as the wild-type using dithionite as reductant. The kcat values of C43S mutant decrease to about 20% of wild-type when reduced B0428 is used as an electron donor
H287A
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very low activity
I289A
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activity comparable to wild-type
I289V
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activity comparable to wild-type
M182T
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activity comparable to wild-type
C273A
mutation in the putative active site cysteine residue, known to coordinate molybdenum binding. NO formation is abolished by the C273A mutation
C114A
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lacks the type I copper ion in the N-terminal domain, shows catalytic activity
C260A
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lacks the type I copper ion in the C-terminal domain, no nitrite-reduction activity
C114A
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lacks the type I copper ion in the N-terminal domain, shows catalytic activity
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C260A
-
lacks the type I copper ion in the C-terminal domain, no nitrite-reduction activity
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H280L
a naturally occuring, enzyme-inactivating mutation in the disease-associated strain i1332, a 9-residues insertion located close to the type I Cu-site and mutation of the catalytic histidine at position 280
M106H
-
inactive protein, the unusual highly cooperative and strongly hysteretic redox titration of the wild-type is lost in the mutant protein
Y25S
-
unlike the wild-type enzyme, the Y25S mutant is active as a reductase toward nitrite, O2, and hydroxylamine without a reduuctive activation step
Y323A
about 90% of wild-type activity. Tether residue Tyr 323 is a gatekeeper for nitrite binding. The water molecules occupying free space above type 2 copper are connected by strong hydrogen bonds, while the channel space, opposite to the NiR-core, is open and contains full occupancy waters
Y323E
about 90% of wild-type activity. Tether residue Tyr 323 is a gatekeeper for nitrite binding. The water molecules occupying free space above type 2 copper are connected by strong hydrogen bonds, while the channel space, opposite to the NiR-core, is open and contains full occupancy waters
Y323F
about 90% of wild-type activity. Tether residue Tyr 323 is a gatekeeper for nitrite binding. Mutant has a single water, W1, bound to the type 2 copper site
Y323A
-
about 90% of wild-type activity. Tether residue Tyr 323 is a gatekeeper for nitrite binding. The water molecules occupying free space above type 2 copper are connected by strong hydrogen bonds, while the channel space, opposite to the NiR-core, is open and contains full occupancy waters
-
Y323E
-
about 90% of wild-type activity. Tether residue Tyr 323 is a gatekeeper for nitrite binding. The water molecules occupying free space above type 2 copper are connected by strong hydrogen bonds, while the channel space, opposite to the NiR-core, is open and contains full occupancy waters
-
Y323F
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about 90% of wild-type activity. Tether residue Tyr 323 is a gatekeeper for nitrite binding. Mutant has a single water, W1, bound to the type 2 copper site
-
M150G
mutant enzyme shows lower catalytic activity than the wild-type enzyme. The type-1 site optical spectrum differs significantly from that of the native enzyme. The midpoint potential of the type-1 site of nitrite reductase M150G is higher than that of the native enzyme
M150G
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mutation increases the reorganization energy by 0.3 eV (30 kJ/mol), binding of the nearby Met62 to the type-1 Cu site lowers the reorganization energy back to approximately the wild-type value
M150T
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mutant enzyme has a type-1 site with a 125-mV higher midpoint potential and a 0.3-eV higher reorganization energy leading to an about 50-fold slower intramolecular electrontransfer to the type-2 site
M150T
mutant enzyme shows lower catalytic activity than the wild-type enzyme
M150T
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mutation increases the reorganization energy by 0.3 eV (30 kJ/mol)
M150G
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mutation increases the reorganization energy by 0.3 eV (30 kJ/mol), binding of the nearby Met62 to the type-1 Cu site lowers the reorganization energy back to approximately the wild-type value
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M150G
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mutant enzyme shows lower catalytic activity than the wild-type enzyme. The type-1 site optical spectrum differs significantly from that of the native enzyme. The midpoint potential of the type-1 site of nitrite reductase M150G is higher than that of the native enzyme
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M150T
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mutation increases the reorganization energy by 0.3 eV (30 kJ/mol)
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M150T
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mutant enzyme shows lower catalytic activity than the wild-type enzyme
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C135A
mutant structure analysis, nitrite bound to the T2 Cu site in the eta1-O end-on form, structure analysis, PDB ID 3WKP
C135A
site-directed mutagenesis, the crystal structure of mutant C135A with nitrite displays a unique eta1-O coordination mode of nitrite at the catalytic copper site (T2Cu) unlike the wild-type enzyme
C135A
in the anaerobic synchrotron-radiation crystallography structure with peroxide bound to the type 2 copper atom, the peroxide molecule is mainly observed in a side-on binding manner, with a possible minor end-on conformation
C135A
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mutant structure analysis, nitrite bound to the T2 Cu site in the eta1-O end-on form, structure analysis, PDB ID 3WKP
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C135A
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site-directed mutagenesis, the crystal structure of mutant C135A with nitrite displays a unique eta1-O coordination mode of nitrite at the catalytic copper site (T2Cu) unlike the wild-type enzyme
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H327A
reduction of nitrite is severely compromised
H327A
mutant protein has no nitrite reductase activity but maintains the ability to reduce O2 to water. Nitrite reductase activity is impaired because of the accumulation of a catalytically inactive form
H327A
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the three-dimensional structures of NIR mutant H327A, and H369A in complex with NO solved by multiple wave-length anomalous dispersion, using the iron anomalous signal, and molecular replacement techniques. In both refined crystal structures the c-heme domain, whilst preserving its classical c-type cytochrome fold, has undergone a 60° rigid-body rotation around an axis parallel with the pseudo 8-fold axis of the beta-propeller, and passing through residue Gln115. Even though the distance between the Fe ions of the c and d1-heme remains 21 A, the edge-to-edge distance between the two hemes has increased by 5 A. Furthermore the distal side of the d1-heme pocket appears to have undergone structural re-arrangement and Tyr10 has moved out of the active site. In the H369A-NO complex, the position and orientation of NO is significantly different from that of the NO bound to the reduced wild-type structure
H369A
reduction of nitrite is severely compromised
H369A
mutant protein has no nitrite reductase activity but maintains the ability to reduce O2 to water. Nitrite reductase activity is impaired because of the accumulation of a catalytically inactive form
H369A
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the three-dimensional structures of NIR mutant H327A, and H369A in complex with NO solved by multiple wave-length anomalous dispersion, using the iron anomalous signal, and molecular replacement techniques. In both refined crystal structures the c-heme domain, whilst preserving its classical c-type cytochrome fold, has undergone a 60° rigid-body rotation around an axis parallel with the pseudo 8-fold axis of the beta-propeller, and passing through residue Gln115. Even though the distance between the Fe ions of the c and d1-heme remains 21 A, the edge-to-edge distance between the two hemes has increased by 5 A. Furthermore the distal side of the d1-heme pocket appears to have undergone structural re-arrangement and Tyr10 has moved out of the active site. In the H369A-NO complex, the position and orientation of NO is significantly different from that of the NO bound to the reduced wild-type structure
H369A
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mutation impairs the reaction with O2, affecting both the properties and lifespan of the intermediate species
Y10F
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no change in optical spectrum, nitrite and oxidase activity and heme c to heme d1 electron transfer rates compared to wild-type
Y10F
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high-field-pulse electron papramagnetic spectroscopy spectra and the derived 14N hyperfine and quadrupole interactions are the same for wild-type and mutant. Residue Y10 does not influence the NO ligand orientation in the reduced state in solution
additional information
replacement of the long 15-residue type 1 copper-binding loop of nitrite reductase with that from Paracoccus versutus cupredoxin amicyanin. The sizable loop contraction does not have a significant effect on the structures of both the type 1 and type 2 CuII sites. The crystal structure of the variant with ZnII at both the type 1 and type 2 sites shows a coordination geometry of the type 2 site that is almost identical to that found in the wild-type protein. In the type 1 centre, the positions of most of the coordinating residues are altered with the largest difference observed for the coordinating His residue in the centre of the mutated loop. This ligand moves away from the active site, which results in a more open metal centre with a coordinating water molecule. The reduction potential of the type i centre is reduced by 200 mV. The resulting unfavourable driving force for electron transfer between the two copper sites, and an increased reorganisation energy for the type 1 centre, contribute to the loop variant having very little nitrite reductase activity
additional information
construction of domain-truncated mutants lacking the Cyt c (18% of wild-type activity) and the Cyt c-Cup domains (3fold increase in activity)
additional information
the core type 1 copper mutant displays a long-range electron tunneling route via a hydrophobic beta-strand, thereby bypassing the type 1 copper core and delivering electrons directly to the catalytic type 2 copper center
additional information
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the core type 1 copper mutant displays a long-range electron tunneling route via a hydrophobic beta-strand, thereby bypassing the type 1 copper core and delivering electrons directly to the catalytic type 2 copper center
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