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ammonium + oxidized ferredoxin + H2O
nitrite + reduced ferredoxin + H+
-
Substrates: -
Products: -
?
hydrogen sulfide + 6 oxidized ferredoxin I [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin I [iron-sulfur] cluster + 6 H+
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
hydrogen sulfide + 6 oxidized methyl viologen [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced methyl viologen [iron-sulfur] cluster + 6 H+
hydrogen sulfide + oxidized ferredoxin + H2O
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized methyl viologen + H2O
sulfite + reduced methyl viologen + H+
Substrates: -
Products: -
?
S-sulfoglutathione + 6 reduced ferredoxin + 6 H+
glutathione persulfide + 6 oxidized ferredoxin + 3 H2O
SO32- + FMNH2
S2- + FMN + H2O
-
Substrates: -
Products: -
?
sulfite + 3 FMNH2
sulfide + 3 FMN + 3 H2O
-
Substrates: sulfate assimilation pathway leading to the biosynthesis of organic sulfur compounds
Products: -
?
sulfite + methyl viologen
sulfide + ?
sulfite + reduced coenzyme F420
sulfide + oxidized coenzyme F420
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
sulfite + reduced ferredoxin + 6 H+
sulfide + oxidized ferredoxin + 3 H2O
-
Substrates: sulfur assimilation for cysteine and methionine biosynthesis
Products: -
?
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
sulfite + reduced methyl viologen + H+
hydrogen sulfide + oxidized methyl viologen + H2O
additional information
?
-
hydrogen sulfide + 6 oxidized ferredoxin I [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin I [iron-sulfur] cluster + 6 H+
Substrates: -
Products: -
?
hydrogen sulfide + 6 oxidized ferredoxin I [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin I [iron-sulfur] cluster + 6 H+
Substrates: -
Products: -
?
hydrogen sulfide + 6 oxidized ferredoxin I [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin I [iron-sulfur] cluster + 6 H+
Substrates: -
Products: -
?
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
Substrates: -
Products: -
?
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
Substrates: -
Products: -
?
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
Substrates: -
Products: -
?
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
Substrates: -
Products: -
?
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
Substrates: -
Products: -
?
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
Substrates: -
Products: -
?
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
Substrates: -
Products: -
?
hydrogen sulfide + 6 oxidized methyl viologen [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced methyl viologen [iron-sulfur] cluster + 6 H+
Substrates: -
Products: -
?
hydrogen sulfide + 6 oxidized methyl viologen [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced methyl viologen [iron-sulfur] cluster + 6 H+
Substrates: -
Products: -
?
hydrogen sulfide + 6 oxidized methyl viologen [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced methyl viologen [iron-sulfur] cluster + 6 H+
Substrates: -
Products: -
?
hydrogen sulfide + oxidized ferredoxin + H2O
sulfite + reduced ferredoxin + H+
-
Substrates: -
Products: -
r
hydrogen sulfide + oxidized ferredoxin + H2O
sulfite + reduced ferredoxin + H+
-
Substrates: -
Products: -
?
hydrogen sulfide + oxidized ferredoxin + H2O
sulfite + reduced ferredoxin + H+
Substrates: -
Products: -
?
S-sulfoglutathione + 6 reduced ferredoxin + 6 H+
glutathione persulfide + 6 oxidized ferredoxin + 3 H2O
-
Substrates: -
Products: -
?
S-sulfoglutathione + 6 reduced ferredoxin + 6 H+
glutathione persulfide + 6 oxidized ferredoxin + 3 H2O
-
Substrates: -
Products: -
?
sulfite + methyl viologen
sulfide + ?
Substrates: -
Products: -
?
sulfite + methyl viologen
sulfide + ?
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: assimilatory sulfate reduction
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: ferredoxin can be partially replaced by benzyl viologen
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: reduced methyl viologen as electron donor also
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: ferredoxin can be partially replaced by benzyl viologen
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: reduced methyl viologen as electron donor also
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
Megalodesulfovibrio gigas
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
Megalodesulfovibrio gigas No. 9332
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
Substrates: PsSiR binds to both double-stranded and single-stranded DNA without significant sequence specificity. DNA binding does not affect the enzymatic activity of PsSiR, suggesting that ferredoxin and sulfite are accessible to SiR molecules within the nucleoids
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: reduced methyl viologen as electron donor also
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: three isoforms of ferredoxin: ferredoxin I, II and III, ferredoxin I and II in leaves, ferredoxin III in roots, ferredoxin I and III shows a comparable ability to donate electrons to enzyme
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: PsSiR binds to both double-stranded and single-stranded DNA without significant sequence specificity. DNA binding does not affect the enzymatic activity of PsSiR, suggesting that ferredoxin and sulfite are accessible to SiR molecules within the nucleoids
Products: -
?
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
Substrates: -
Products: -
?
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
r
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
Substrates: -
Products: -
?
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
Substrates: -
Products: -
?
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
Substrates: -
Products: -
?
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
r
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
r
sulfite + reduced methyl viologen + H+
hydrogen sulfide + oxidized methyl viologen + H2O
-
Substrates: -
Products: -
?
sulfite + reduced methyl viologen + H+
hydrogen sulfide + oxidized methyl viologen + H2O
-
Substrates: -
Products: -
?
sulfite + reduced methyl viologen + H+
hydrogen sulfide + oxidized methyl viologen + H2O
-
Substrates: -
Products: -
r
additional information
?
-
-
Substrates: enzyme activites of shoot and root increase by sulfate limitation in the early stage of growth
Products: -
?
additional information
?
-
-
Substrates: no activity with NADPH as single electron donor
Products: -
?
additional information
?
-
Substrates: enzyme additionally shows activity of nitrite reductase, EC 1.7.7.1
Products: -
?
additional information
?
-
Substrates: enzyme additionally shows activity of nitrite reductase, EC 1.7.7.1
Products: -
?
additional information
?
-
-
Substrates: enzyme additionally shows activity of nitrite reductase, EC 1.7.7.1
Products: -
?
additional information
?
-
Substrates: enzyme additionally shows activity of nitrite reductase, EC 1.7.7.1
Products: -
?
additional information
?
-
Substrates: enzyme additionally shows activity of nitrite reductase, EC 1.7.7.1
Products: -
?
additional information
?
-
Substrates: NirA has a pronounced preference for sulfite over nitrite as substrate
Products: -
?
additional information
?
-
-
Substrates: NirA has a pronounced preference for sulfite over nitrite as substrate
Products: -
?
additional information
?
-
Substrates: NirA has a pronounced preference for sulfite over nitrite as substrate
Products: -
?
additional information
?
-
-
Substrates: no activity with NADPH as single electron donor
Products: -
?
additional information
?
-
Substrates: ferredoxin:SiR complex formation and interprotein affinity are thermodynamically adjusted by both enthalpy and entropy through electrostatic and non-electrostatic interactions. A combination of electrostatic and non-electrostatic forces stabilizes the complex with similar interfaces and modulates the binding affinity and mode
Products: -
?
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hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
hydrogen sulfide + oxidized ferredoxin + H2O
sulfite + reduced ferredoxin + H+
-
Substrates: -
Products: -
?
sulfite + 3 FMNH2
sulfide + 3 FMN + 3 H2O
-
Substrates: sulfate assimilation pathway leading to the biosynthesis of organic sulfur compounds
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
sulfite + reduced ferredoxin + 6 H+
sulfide + oxidized ferredoxin + 3 H2O
-
Substrates: sulfur assimilation for cysteine and methionine biosynthesis
Products: -
?
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
Substrates: -
Products: -
?
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
Substrates: -
Products: -
?
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
Substrates: -
Products: -
?
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
Substrates: -
Products: -
?
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
Substrates: -
Products: -
?
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
Substrates: -
Products: -
?
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: assimilatory sulfate reduction
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
Megalodesulfovibrio gigas
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
Megalodesulfovibrio gigas No. 9332
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
Substrates: -
Products: -
?
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
-
Substrates: -
Products: -
?
sulfite + reduced ferredoxin + H+
hydrogen sulfide + oxidized ferredoxin + H2O
Substrates: -
Products: -
?
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evolution
the common feature of both assimilatory and dissimilatory sulfite reductases is that they share a highly conserved domain C-X5-C-n-C-X3-C for binding the siroheme and the [4Fe-4S] cluster. In addition to these two class of sulfite reductases there exists a third class of assimilatory sulfite reductase found in a number of strictly anaerobic bacteria, cf. EC 1.8.1.2 and EC 1.8.99.5
evolution
-
the common feature of both assimilatory and dissimilatory sulfite reductases is that they share a highly conserved domain C-X5-C-n-C-X3-C for binding the siroheme and the [4Fe-4S] cluster. In addition to these two class of sulfite reductases there exists a third class of assimilatory sulfite reductase found in a number of strictly anaerobic bacteria, cf. EC 1.8.1.2 and EC 1.8.99.5
-
evolution
-
the common feature of both assimilatory and dissimilatory sulfite reductases is that they share a highly conserved domain C-X5-C-n-C-X3-C for binding the siroheme and the [4Fe-4S] cluster. In addition to these two class of sulfite reductases there exists a third class of assimilatory sulfite reductase found in a number of strictly anaerobic bacteria, cf. EC 1.8.1.2 and EC 1.8.99.5
-
malfunction
-
depletion of the enzyme results in chloroplast ablation
malfunction
wild-type FdSiR and mutant FdSiRC491G in the presence of the artificial electron donor methyl viologen are both able to reduce sulfite to H2S, but the detected lower rate of H2S evolution for mutant FdSiRC491G is likely related to its lower cofactor content
malfunction
-
wild-type FdSiR and mutant FdSiRC491G in the presence of the artificial electron donor methyl viologen are both able to reduce sulfite to H2S, but the detected lower rate of H2S evolution for mutant FdSiRC491G is likely related to its lower cofactor content
-
malfunction
-
wild-type FdSiR and mutant FdSiRC491G in the presence of the artificial electron donor methyl viologen are both able to reduce sulfite to H2S, but the detected lower rate of H2S evolution for mutant FdSiRC491G is likely related to its lower cofactor content
-
metabolism
-
in addition to participating in the sulfate assimilation reductive pathway, the enzyme also plays a role in protecting leaves against the toxicity of sulfite accumulation
metabolism
in addition to participating in the sulfate assimilation reductive pathway, the enzyme also plays a role in protecting leaves against the toxicity of sulfite accumulation
physiological function
-
the enzyme plays a role in chloroplast-nucleoid metabolism, plastid gene expression, and thylakoid membrane development
physiological function
ferredoxin sulfite reductase (FdSiR) catalyzes the six-electron reduction of sulfite to hydrogen sulfite and nitrite to ammonia
physiological function
the life cycle of Prochlorococcus marinus is influenced by viruses. Cyanophages that infect it have evolved genomes with as many as 327 open reading frames (ORFs). Viruses from three clades infect Prochlorococcus marinus, including T4-like myoviruses, T7-like podoviruses, and, less commonly, members of Siphoviridae. In some ecosystems, as many as 50% of cyanobacteria may be infected at any point in time. The sulfite reductase from Prochlorococcus marinus can utilize, besides its endogenous ferredoxin, also the phage ferredoxin, pssm2-Fd, from its parasite myovirus P-SSM2
physiological function
-
ferredoxin sulfite reductase (FdSiR) catalyzes the six-electron reduction of sulfite to hydrogen sulfite and nitrite to ammonia
-
physiological function
-
the life cycle of Prochlorococcus marinus is influenced by viruses. Cyanophages that infect it have evolved genomes with as many as 327 open reading frames (ORFs). Viruses from three clades infect Prochlorococcus marinus, including T4-like myoviruses, T7-like podoviruses, and, less commonly, members of Siphoviridae. In some ecosystems, as many as 50% of cyanobacteria may be infected at any point in time. The sulfite reductase from Prochlorococcus marinus can utilize, besides its endogenous ferredoxin, also the phage ferredoxin, pssm2-Fd, from its parasite myovirus P-SSM2
-
physiological function
-
the life cycle of Prochlorococcus marinus is influenced by viruses. Cyanophages that infect it have evolved genomes with as many as 327 open reading frames (ORFs). Viruses from three clades infect Prochlorococcus marinus, including T4-like myoviruses, T7-like podoviruses, and, less commonly, members of Siphoviridae. In some ecosystems, as many as 50% of cyanobacteria may be infected at any point in time. The sulfite reductase from Prochlorococcus marinus can utilize, besides its endogenous ferredoxin, also the phage ferredoxin, pssm2-Fd, from its parasite myovirus P-SSM2
-
physiological function
-
the life cycle of Prochlorococcus marinus is influenced by viruses. Cyanophages that infect it have evolved genomes with as many as 327 open reading frames (ORFs). Viruses from three clades infect Prochlorococcus marinus, including T4-like myoviruses, T7-like podoviruses, and, less commonly, members of Siphoviridae. In some ecosystems, as many as 50% of cyanobacteria may be infected at any point in time. The sulfite reductase from Prochlorococcus marinus can utilize, besides its endogenous ferredoxin, also the phage ferredoxin, pssm2-Fd, from its parasite myovirus P-SSM2
-
physiological function
-
ferredoxin sulfite reductase (FdSiR) catalyzes the six-electron reduction of sulfite to hydrogen sulfite and nitrite to ammonia
-
additional information
the enzyme contains a [4Fe-4S]2+/1+ cluster and a siroheme active site
additional information
-
the enzyme contains a [4Fe-4S]2+/1+ cluster and a siroheme active site
-
additional information
-
the enzyme contains a [4Fe-4S]2+/1+ cluster and a siroheme active site
-
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G212S/L213T/Y214L/S217C/C220I/S221N
mutations mimic partially isoform SiRA
S217C
mutation mimics the corresponding residue in isoform SiRA, recovers sulfite reduction activity
G212S/L213T/Y214L/S217C/C220I/S221N
-
mutations mimic partially isoform SiRA
-
S217C
-
mutation mimics the corresponding residue in isoform SiRA, recovers sulfite reduction activity
-
C161A
catalytically impaired mutant, tested in an assay using the nonphysiological electron donor methyl viologen and sulfite as substrate
C161S
catalytically impaired mutant, tested in an assay using the nonphysiological electron donor methyl viologen and sulfite as substrate
Y69A
catalytically impaired mutant, tested in an assay using the nonphysiological electron donor methyl viologen and sulfite as substrate
Y69F
catalytically impaired mutant, tested in an assay using the nonphysiological electron donor methyl viologen and sulfite as substrate
C161A
-
catalytically impaired mutant, tested in an assay using the nonphysiological electron donor methyl viologen and sulfite as substrate
-
C161S
-
catalytically impaired mutant, tested in an assay using the nonphysiological electron donor methyl viologen and sulfite as substrate
-
Y69A
-
catalytically impaired mutant, tested in an assay using the nonphysiological electron donor methyl viologen and sulfite as substrate
-
Y69F
-
catalytically impaired mutant, tested in an assay using the nonphysiological electron donor methyl viologen and sulfite as substrate
-
A493G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
A503G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Arg111Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Arg114Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Arg324Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
L499G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
L502A
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Lys117Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Lys582Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Lys584Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
Lys66Q
remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme
P501G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
P541G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
Q504G
mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity
C491G
site-directed mutagenesis, the mutant shows a lower rate of H2S evolution compared to wild-type likely related to its lower cofactor content. The mutagenesis of this Cys residue to a Gly opens an exchangeable coordination site to a corner iron atom that can be chemically rescued by an external thiolate ligand. This ligand can be subsequently displaced by mass action using a dithiol molecular wire to tether two redox active proteins. Application of this technique to tethering Photosystem I to ferredoxin sulfite reductase (FdSiR). UV/Vis absorbance spectra of both FdSiRWT and the FdSiRC491G variant display characteristic peaks at 278, 392 (Soret), 585 (alpha) and 714 nm (charge transfer band), and 278, 394 (Soret), 587 (alpha) and 714 nm (charge transfer band) respectively. Both enzymes in their as-isolated forms display an EPR spectrum characteristic of an S=5/2 high spin heme. When reduced, both enzymes exhibit the signal of a low spin S=1/2 [4Fe-4S]1+ cluster. The FdSiRWT and FdSiRC491G variant both show activity using reduced methyl viologen and Synechococcus elongatus PCC 7942 ferredoxin 1 (Fd1) as electron donors. Based on these results, the FdSIRC491G variant should be a suitable candidate for wiring to Photosystem I
C491G
-
site-directed mutagenesis, the mutant shows a lower rate of H2S evolution compared to wild-type likely related to its lower cofactor content. The mutagenesis of this Cys residue to a Gly opens an exchangeable coordination site to a corner iron atom that can be chemically rescued by an external thiolate ligand. This ligand can be subsequently displaced by mass action using a dithiol molecular wire to tether two redox active proteins. Application of this technique to tethering Photosystem I to ferredoxin sulfite reductase (FdSiR). UV/Vis absorbance spectra of both FdSiRWT and the FdSiRC491G variant display characteristic peaks at 278, 392 (Soret), 585 (alpha) and 714 nm (charge transfer band), and 278, 394 (Soret), 587 (alpha) and 714 nm (charge transfer band) respectively. Both enzymes in their as-isolated forms display an EPR spectrum characteristic of an S=5/2 high spin heme. When reduced, both enzymes exhibit the signal of a low spin S=1/2 [4Fe-4S]1+ cluster. The FdSiRWT and FdSiRC491G variant both show activity using reduced methyl viologen and Synechococcus elongatus PCC 7942 ferredoxin 1 (Fd1) as electron donors. Based on these results, the FdSIRC491G variant should be a suitable candidate for wiring to Photosystem I
-
C491G
-
site-directed mutagenesis, the mutant shows a lower rate of H2S evolution compared to wild-type likely related to its lower cofactor content. The mutagenesis of this Cys residue to a Gly opens an exchangeable coordination site to a corner iron atom that can be chemically rescued by an external thiolate ligand. This ligand can be subsequently displaced by mass action using a dithiol molecular wire to tether two redox active proteins. Application of this technique to tethering Photosystem I to ferredoxin sulfite reductase (FdSiR). UV/Vis absorbance spectra of both FdSiRWT and the FdSiRC491G variant display characteristic peaks at 278, 392 (Soret), 585 (alpha) and 714 nm (charge transfer band), and 278, 394 (Soret), 587 (alpha) and 714 nm (charge transfer band) respectively. Both enzymes in their as-isolated forms display an EPR spectrum characteristic of an S=5/2 high spin heme. When reduced, both enzymes exhibit the signal of a low spin S=1/2 [4Fe-4S]1+ cluster. The FdSiRWT and FdSiRC491G variant both show activity using reduced methyl viologen and Synechococcus elongatus PCC 7942 ferredoxin 1 (Fd1) as electron donors. Based on these results, the FdSIRC491G variant should be a suitable candidate for wiring to Photosystem I
-
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