1.7.2.4: nitrous-oxide reductase
This is an abbreviated version!
For detailed information about nitrous-oxide reductase, go to the full flat file.
Word Map on EC 1.7.2.4
-
1.7.2.4
-
denitrification
-
denitrify
-
nitrite
-
greenhouse
-
denitrificans
-
paracoccus
-
stutzeri
-
dinitrogen
-
wastewater
-
binuclear
-
tetranuclear
-
cycloclastes
-
mixed-valence
-
multicopper
-
ammonia-oxidizing
-
n-cycle
-
nautica
-
wolinella
-
arable
-
nitrospirae
-
stratospheric
-
agriculture
-
t-rflp
-
degradation
- 1.7.2.4
-
denitrification
-
denitrify
- nitrite
-
greenhouse
- denitrificans
- paracoccus
- stutzeri
-
dinitrogen
-
wastewater
-
binuclear
-
tetranuclear
- cycloclastes
-
mixed-valence
-
multicopper
-
ammonia-oxidizing
-
n-cycle
- nautica
-
wolinella
-
arable
- nitrospirae
-
stratospheric
- agriculture
-
t-rflp
- degradation
Reaction
+ + = + 2 ferrocytochrome c + 2 H+
Synonyms
cNosZ, EC 1.7.99.6, HdN2OR, McoP, MhN2OR, multicopper oxidase, N(2)OR, N2O reductase, N2OR, nitrous oxide reductase, NosZ, PpN2OR, PsN2OR, Sden_2219, SdN2OR, Z-type N2OR
ECTree
Advanced search results
Metals Ions
Metals Ions on EC 1.7.2.4 - nitrous-oxide reductase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Ca2+
copper
Cu
Cu2+
Ca2+
single Ca2+ ion binds to the Ca2+-binding loop coordinated by residues Y251, E255, M263, D269, and S316 and a water molecule, Ca2+ plays a role in secondary structure stabilization during maturation of nitrous oxide reductase, required for structural stability of the binuclear CuA site
-
the fully reduced all-Cu(I) state of CuZ is the catalytically relevant redox state of N2OR
copper
-
form A and B contain 9.0 and 8.2 Cu atoms per dimer, respectively
copper
N2OR contains two copper centers, CuA, a binuclear mixed-valence center and CuZ, a tetranuclear sulfide-bridged copper cluster
copper
-
dependent on. The enzyme nitrous oxide reductase contains two copper sites: a binuclear site known as CuA that functions as an electron transfer site, and an unusual tetranuclear copper sulfide cluster active site, where N2O binds and is reduced. Two forms of this tetranuclear site have been structurally characterized. One, known as CuZ*, has a mu4 sulfide ligand bridging all four coppers and a solvent derived ligand on an open edge (the CuI-CuIV edge) where N2O is proposed to bind. The other form of the cluster, known as CuZ, has an additional mu2 sulfur ligand bridging the CuI-CuIV edge. Raman spectroscopic analysis and computationa modelling of Cu site structure and mechanism, binding and interaction, overview. Protonation state of the mu2 sulfur ligand on the CuI-CuIV edge in 1-hole and 2-hole CuZ
copper
-
multicopper enzyme, 2 copper centers per subunit, CuA and CuZ
copper
-
dependent on. The enzyme nitrous oxide reductase contains two copper sites: a binuclear site known as CuA that functions as an electron transfer site, and an unusual tetranuclear copper sulfide cluster active site, where N2O binds and is reduced. Two forms of this tetranuclear site have been structurally characterized. One, known as CuZ*, has a mu4 sulfide ligand bridging all four coppers and a solvent derived ligand on an open edge (the CuI-CuIV edge) where N2O is proposed to bind. The other form of the cluster, known as CuZ, has an additional mu2 sulfur ligand bridging the CuI-CuIV edge. Raman spectroscopic analysis and computationa modelling of Cu site structure and mechanism, binding and interaction, overview. Protonation state of the mu2 sulfur ligand on the CuI-CuIV edge in 1-hole and 2-hole CuZ
copper
-
3.2 mol of copper per mol of enzyme, in the as-isolated form. Presence of 0.1 mM enhances enzymic activity by 2fold
Cu
-
Cu is bound by apo NosL, a coexpressed protein which is necessary for the assembling process of nitrous oxide reductase
Cu
-
A monomer carries 2 copper centers: CuA, which is a binuclear mixed-valence center similar to the CuA of cytochrome oxidases,4 and CuZ, a tetranuclear sulfidebridged copper cluster.
Cu
Marinobacter nauticus
-
six copper atoms per monomer arranged in two centers named CuA and CuZ, 10.7 atoms per dimer
Cu
Marinobacter nauticus
two copper binding sites. The Cu4S active site is ligated by 7 His residues and contains three copper atoms (designated CuI, CuII, and CuIV) that share a plane with the mu4 sulfide ligand and with a solvent-derived ligand that bridges the CuI?CuIV edge, while the fourth copper (CuIII) bound to the mu4S2- is oriented out of this plane. Spectroscopic definition of the resting state of the Cu4S cluster, CuZ* intermediate, in turnover of nitrous oxide. CuZ°, an intermediate form of the Cu4S active site of nitrous oxide reductase (N2OR) is observed in single turnover of fully reduced N2OR with N2O, geometric and electronic structure, overview. CuZ° is a 1-hole (i.e. 3CuICuII) state with spin density delocalized evenly over CuI and CuIV. CuZ° has a terminal hydroxide ligand coordinated to CuIV, stabilized by a hydrogen bond to a nearby lysine residue. CuZ° can be reduced via electron transfer from CuA using a physiologically relevant reductant. Computational modelling of the Cu4S active site built from the atomic coordinates of the crystal structure of PdN2OR, PDB ID 1FWX at 1.6 A resolution, The model includes the active site core (Cu4S), the edge hydroxide, seven ligating histidines, and the second sphere residues Lys397 and Glu435. Spectrocopic Cu binding structure analysis, overview. reduction of CuZ° via electron transfer from CuA in turnover with cytrochrome c552 is faster than the decay of CuZ° to the inactive resting 1-hole CuZ* state of the Cu4S cluster, indicating that N2O reduction by the Cu4S active site of N2OR bypasses the resting 1-hole CuZ* state, which is not reduced by physiologically relevant reductants, instead, the 1-hole CuZ° intermediate is the relevant 1-hole oxidized state of the Cu4S cluster during turnover
Cu
-
one dinuclear centre CuA and a copper cluster CuZ in which four copper ions are litigated by seven histidine imidazoles and a bridging inorganic sufide
Cu
-
one dinuclear centre CuA and a copper cluster CuZ in which four copper ions are litigated by seven histidine imidazoles and a bridging inorganic sufide
Cu
-
CuA can exist in two oxidation forms [Cu1.5+ - Cu1.5+] and [Cu1+ - Cu1+]
Cu
-
N2OR contains two metal centers: a binuclear copper center, CuA, that serves to receive electrons from soluble donors, and a tetranuclear copper-sulfide center, CuZ, at the active site.
Cu
-
The two copper atoms (CuI and CuIV) at the ligand-binding site of the cluster play a crucial role in the enzymatic function, as these atoms are directly involved in bridged N2O binding.
a copper enzyme, conformational changes of the CuA center may affect electron transfer from the physiological electron donor and the electron-transfer rate from CuA to CuZ, overview
Cu2+
a copper enzyme, two copper centers, CuA and CuB, per monomer, binding structure, detailed analysis of the pH effect at the CuZ site, e.g. using spectroscopic and computational methods, overview
Cu2+
the enzyme contains average 4.5 Cu and 1.2 S per monomer
Cu2+
Marinobacter nauticus
a copper enzyme, two copper centers, CuA and CuB, binding structure, detailed analysis of the pH effect at the CuZ site, e.g. using spectroscopic and computational methods, overview
Cu2+
Marinobacter nauticus
-
enzyme isolated from cells grown at pH 6.5 has its catalytic center mainly as CuZ(4Cu1S), while that from cells grown at pH 7.5 or 8.5 has it as CuZ(4Cu2S)
Cu2+
a copper enzyme with cupredoxin containing blue T1 copper and red T2 copper. Blue and red copper centers form initially before they are pH-dependently transformed into purple CuA center, lower pH resulting in fewer trapped T1 and T2 coppers and faster transition
Cu2+
-
bound in a Cu centre, dependent on. The state of Cuz in extracted N2OR depends on the conditions during purification. Anoxic purification yields the purple, active form of the enzyme, whereas oxic conditions results in a blue form of N2OR with a redox inert Cuz centre, Cuz*. The blue form of N2OR is catalytically inactive, but may be reactivated in vitro by a strong reductant such as reduced methyl viologen
Cu2+
the enzyme contains a tetranuclear copper-sulfide center consisting of the binuclear mixed-valent CuA center that acts as the electron transferring center, and the catalytic center, CuZ
Cu2+
the multicopper enzyme contains a CuA and a tetranuclear copper sulfide-bridged CuZ center
Cu2+
-
the copper enzyme contains an unusual mixed valence copper, Cu(I)/Cu(II), dimer centre, the primary paramagnetic species is the CuA, the catalytic CuZ centre being primarily in a diamagnetic oxidized form. Coherent Raman detected electron spin resonance spectroscopy structure analysis of the CuA site in nitrous oxide reductase, overview
Cu2+
involved in catalysis. In the absence of Ca2+, substantial parts of the enzyme surrounding the binding sites for the copper ions show structural disorder. Reconstitution of the binuclear CuA site was possible in vitro but required the presence of Ca2+ ions for a stable insertion of the center
Cu2+
Stutzerimonas stutzeri
the enzyme contains a tetranuclear copper-sulfide center consisting of the binuclear mixed-valent CuA center that acts as the electron transferring center, and the catalytic center, CuZ
Cu2+
Stutzerimonas stutzeri
the enzyme has a mixed-valent Cys-bridged [Cu1.5+(CyS)2Cu1.5+] copper site
Cu2+
Stutzerimonas stutzeri
the multicopper enzyme contains a CuA and a tetranuclear copper sulfide-bridged CuZ center
Cu2+
-
the active site for catalytic N2O reduction in the enzyme is a tetranuclear copper cluster
Cu2+
-
the enzyme contains a tetranuclear copper-sulfide center consisting of the binuclear mixed-valent CuA center that acts as the electron transferring center, and the catalytic center, CuZ