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N2O + 2 Fe2+ + 2 H+
N2 + H2O + 2 Fe3+
-
-
-
-
?
N2O + H2O + benzyl viologen cation radical
N2 + reduced benzyl viologen
N2O + reduced acceptor
N2 + H2O + acceptor
N2O + reduced benzyl viologen
N2 + H2O + benzyl viologen
N2O + reduced benzyl viologen
N2 + oxidized benzyl viologen
-
-
-
?
N2O + reduced cytochrome c
N2 + H2O + cytochrome c
-
-
-
-
?
N2O + reduced cytochrome c550
N2 + H2O + cytochrome c550
N2O + reduced methyl viologen
N2 + H2O + methyl viologen
N2O + reduced methyl viologen
N2 + H2O + oxidized methyl viologen
Marinobacter nauticus
-
-
-
-
?
N2O + reduced methyl viologen
N2 + oxidized methyl viologen
N2O + reduced pseudoazurin
N2 + H2O + pseudoazurin
N2O + reduced pseudoazurin
N2 + oxidized pseudoazurin
blue copper electron-transfer protein pseudoazurin is capable of mediating electron transfer to the nitrous oxide reductase. Pseudoazurin binds near copper site CuA, with parameters consistent with the formation of a transient, weakly-bound complex. Pseudoazurin a strong candidate for the physiological electron donor to th enzyme
-
-
?
nitrogen + H2O + 2 ferricytochrome c
nitrous oxide + 2 ferrocytochrome c + 2 H+
Stutzerimonas stutzeri
-
-
-
?
nitrogen + H2O + acceptor
nitrous oxide + reduced acceptor
nitrous oxide + 2 ferrocytochrome c + 2 H+
nitrogen + H2O + 2 ferricytochrome c
nitrous oxide + 2 reduced cytochrome c
nitrogen + H2O + 2 cytochrome c
nitrous oxide + 2 reduced methyl viologen
nitrogen + H2O + 2 methyl viologen
nitrous oxide + benzyl viologen + H+
nitrogen + oxidized benzyl viologen + H2O
Stutzerimonas stutzeri
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
nitrous oxide + reduced benzyl viologen + H+
nitrogen + H2O + oxidized benzyl viologen
-
-
-
-
r
nitrous oxide + reduced methyl viologen
nitrogen + H2O + methyl viologen
nitrous oxide + reduced methyl viologen + H+
nitrogen + H2O + oxidized methyl viologen
-
-
-
-
r
additional information
?
-
N2O + H2O + benzyl viologen cation radical
N2 + reduced benzyl viologen
-
-
-
-
?
N2O + H2O + benzyl viologen cation radical
N2 + reduced benzyl viologen
-
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
-
?
N2O + reduced benzyl viologen
N2 + H2O + benzyl viologen
-
-
-
-
?
N2O + reduced benzyl viologen
N2 + H2O + benzyl viologen
-
-
-
-
?
N2O + reduced benzyl viologen
N2 + H2O + benzyl viologen
-
-
-
-
?
N2O + reduced benzyl viologen
N2 + H2O + benzyl viologen
-
-
-
-
?
N2O + reduced cytochrome c550
N2 + H2O + cytochrome c550
-
-
-
-
?
N2O + reduced cytochrome c550
N2 + H2O + cytochrome c550
-
-
-
?
N2O + reduced methyl viologen
N2 + H2O + methyl viologen
-
-
-
-
?
N2O + reduced methyl viologen
N2 + H2O + methyl viologen
-
-
-
-
?
N2O + reduced methyl viologen
N2 + oxidized methyl viologen
-
-
-
?
N2O + reduced methyl viologen
N2 + oxidized methyl viologen
-
-
-
?
N2O + reduced pseudoazurin
N2 + H2O + pseudoazurin
-
-
-
-
?
N2O + reduced pseudoazurin
N2 + H2O + pseudoazurin
-
-
-
?
nitrogen + H2O + acceptor
nitrous oxide + reduced acceptor
-
-
-
?
nitrogen + H2O + acceptor
nitrous oxide + reduced acceptor
under some conditions, electron transfer may be rate limiting in N2O reduction. The transition state is stabilized by H-bonding interactions between the active site and an N2O-derived intermediate bound to the catalytic CuZ cluster
-
-
?
nitrogen + H2O + acceptor
nitrous oxide + reduced acceptor
-
-
-
-
?
nitrous oxide + 2 ferrocytochrome c + 2 H+
nitrogen + H2O + 2 ferricytochrome c
-
-
-
-
?
nitrous oxide + 2 ferrocytochrome c + 2 H+
nitrogen + H2O + 2 ferricytochrome c
-
-
-
-
?
nitrous oxide + 2 ferrocytochrome c + 2 H+
nitrogen + H2O + 2 ferricytochrome c
Marinobacter nauticus
-
-
-
-
?
nitrous oxide + 2 ferrocytochrome c + 2 H+
nitrogen + H2O + 2 ferricytochrome c
-
-
-
?
nitrous oxide + 2 ferrocytochrome c + 2 H+
nitrogen + H2O + 2 ferricytochrome c
-
-
-
?
nitrous oxide + 2 ferrocytochrome c + 2 H+
nitrogen + H2O + 2 ferricytochrome c
Stutzerimonas stutzeri
-
-
-
?
nitrous oxide + 2 ferrocytochrome c + 2 H+
nitrogen + H2O + 2 ferricytochrome c
-
-
-
-
?
nitrous oxide + 2 ferrocytochrome c + 2 H+
nitrogen + H2O + 2 ferricytochrome c
-
-
-
-
?
nitrous oxide + 2 ferrocytochrome c + 2 H+
nitrogen + H2O + 2 ferricytochrome c
-
-
-
-
?
nitrous oxide + 2 reduced cytochrome c
nitrogen + H2O + 2 cytochrome c
-
-
-
?
nitrous oxide + 2 reduced cytochrome c
nitrogen + H2O + 2 cytochrome c
-
-
-
?
nitrous oxide + 2 reduced cytochrome c
nitrogen + H2O + 2 cytochrome c
Marinobacter nauticus
-
-
-
?
nitrous oxide + 2 reduced cytochrome c
nitrogen + H2O + 2 cytochrome c
Marinobacter nauticus 617
-
-
-
?
nitrous oxide + 2 reduced cytochrome c
nitrogen + H2O + 2 cytochrome c
-
-
-
-
?
nitrous oxide + 2 reduced cytochrome c
nitrogen + H2O + 2 cytochrome c
-
-
-
?
nitrous oxide + 2 reduced cytochrome c
nitrogen + H2O + 2 cytochrome c
the copper enzyme nitrous oxide reductase catalyzes the two-electron reduction of nitrous oxide (N2O) to dinitrogen
-
-
?
nitrous oxide + 2 reduced cytochrome c
nitrogen + H2O + 2 cytochrome c
-
-
-
?
nitrous oxide + 2 reduced cytochrome c
nitrogen + H2O + 2 cytochrome c
the copper enzyme nitrous oxide reductase catalyzes the two-electron reduction of nitrous oxide (N2O) to dinitrogen
-
-
?
nitrous oxide + 2 reduced cytochrome c
nitrogen + H2O + 2 cytochrome c
-
-
-
-
?
nitrous oxide + 2 reduced cytochrome c
nitrogen + H2O + 2 cytochrome c
-
-
-
-
?
nitrous oxide + 2 reduced cytochrome c
nitrogen + H2O + 2 cytochrome c
-
-
-
?
nitrous oxide + 2 reduced methyl viologen
nitrogen + H2O + 2 methyl viologen
Marinobacter nauticus
-
-
-
?
nitrous oxide + 2 reduced methyl viologen
nitrogen + H2O + 2 methyl viologen
Marinobacter nauticus 617
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
methyl viologen as electron donor
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
dithionite-reduced methyl viologen as electron donor
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
photochemically-reduced benzyl viologen as electron donor
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
photochemically reduced benzyl viologen and 3,3',5,5'-tetramethylbenzidine as electron donor
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
dithionite-reduced benzyl viologen as electron donor
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
Marinobacter nauticus
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
Marinobacter nauticus 617
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
methyl viologen as electron donor
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
photochemically-reduced benzyl viologen as electron donor
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
a mixture of N,N,N',N'-tetramethyl-p-phenylenediamine and ascorbate as electron donor
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
methyl viologen as electron donor, activity after incubation with ferricyanide, ascorbate or dithionite
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
dithionite-reduced methyl viologen as electron donor
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
dithionite-reduced methyl viologen as electron donor
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
photochemically-reduced benzyl viologen as electron donor
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
methyl viologen as electron donor
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
photochemically-reduced benzyl viologen as electron donor
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
photochemically-reduced benzyl viologen as electron donor
-
-
?
nitrous oxide + reduced methyl viologen
nitrogen + H2O + methyl viologen
-
-
-
?
nitrous oxide + reduced methyl viologen
nitrogen + H2O + methyl viologen
-
-
-
?
additional information
?
-
Marinobacter nauticus
-
the purple form of enzyme, in which the copper centre is in the oxidized [2Cu2+:2Cu+] redox state, is redox active, although it is still catalytically non-competent, as its specific activity is lower than that of the activated fully reduced enzyme and comparable with that of the enzyme with the copper centre in either the [1Cu2+:3Cu+] redox state or in the redox inactive state
-
-
?
additional information
?
-
-
determination of detailed gas kinetics and transcription patterns from batch culture experiments with Paracoccus denitrificans, allowing in vivo estimation of electron flow to O2 and N2O under various O2 regimes
-
-
?
additional information
?
-
-
enzyme shows Cu+/Fe2+ oxidation kinetics that follow the Michaelis-Menten model, with 2fold to 10fold higher efficiencies for Cu+ and Fe2+ as compared with the tested aromatic compounds
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
N2O + reduced acceptor
N2 + H2O + acceptor
N2O + reduced pseudoazurin
N2 + oxidized pseudoazurin
blue copper electron-transfer protein pseudoazurin is capable of mediating electron transfer to the nitrous oxide reductase. Pseudoazurin binds near copper site CuA, with parameters consistent with the formation of a transient, weakly-bound complex. Pseudoazurin a strong candidate for the physiological electron donor to th enzyme
-
-
?
nitrogen + H2O + 2 ferricytochrome c
nitrous oxide + 2 ferrocytochrome c + 2 H+
Stutzerimonas stutzeri
-
-
-
?
nitrogen + H2O + acceptor
nitrous oxide + reduced acceptor
-
-
-
?
nitrous oxide + 2 ferrocytochrome c + 2 H+
nitrogen + H2O + 2 ferricytochrome c
nitrous oxide + 2 reduced cytochrome c
nitrogen + H2O + 2 cytochrome c
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
nitrous oxide + reduced methyl viologen
nitrogen + H2O + methyl viologen
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
?
N2O + reduced acceptor
N2 + H2O + acceptor
-
-
-
-
?
nitrous oxide + 2 ferrocytochrome c + 2 H+
nitrogen + H2O + 2 ferricytochrome c
-
-
-
-
?
nitrous oxide + 2 ferrocytochrome c + 2 H+
nitrogen + H2O + 2 ferricytochrome c
-
-
-
-
?
nitrous oxide + 2 ferrocytochrome c + 2 H+
nitrogen + H2O + 2 ferricytochrome c
Marinobacter nauticus
-
-
-
-
?
nitrous oxide + 2 ferrocytochrome c + 2 H+
nitrogen + H2O + 2 ferricytochrome c
-
-
-
?
nitrous oxide + 2 ferrocytochrome c + 2 H+
nitrogen + H2O + 2 ferricytochrome c
-
-
-
?
nitrous oxide + 2 ferrocytochrome c + 2 H+
nitrogen + H2O + 2 ferricytochrome c
Stutzerimonas stutzeri
-
-
-
?
nitrous oxide + 2 ferrocytochrome c + 2 H+
nitrogen + H2O + 2 ferricytochrome c
-
-
-
-
?
nitrous oxide + 2 ferrocytochrome c + 2 H+
nitrogen + H2O + 2 ferricytochrome c
-
-
-
-
?
nitrous oxide + 2 ferrocytochrome c + 2 H+
nitrogen + H2O + 2 ferricytochrome c
-
-
-
-
?
nitrous oxide + 2 reduced cytochrome c
nitrogen + H2O + 2 cytochrome c
-
-
-
?
nitrous oxide + 2 reduced cytochrome c
nitrogen + H2O + 2 cytochrome c
-
-
-
?
nitrous oxide + 2 reduced cytochrome c
nitrogen + H2O + 2 cytochrome c
Marinobacter nauticus
-
-
-
?
nitrous oxide + 2 reduced cytochrome c
nitrogen + H2O + 2 cytochrome c
Marinobacter nauticus 617
-
-
-
?
nitrous oxide + 2 reduced cytochrome c
nitrogen + H2O + 2 cytochrome c
-
-
-
-
?
nitrous oxide + 2 reduced cytochrome c
nitrogen + H2O + 2 cytochrome c
-
-
-
?
nitrous oxide + 2 reduced cytochrome c
nitrogen + H2O + 2 cytochrome c
-
-
-
?
nitrous oxide + 2 reduced cytochrome c
nitrogen + H2O + 2 cytochrome c
-
-
-
-
?
nitrous oxide + 2 reduced cytochrome c
nitrogen + H2O + 2 cytochrome c
-
-
-
-
?
nitrous oxide + 2 reduced cytochrome c
nitrogen + H2O + 2 cytochrome c
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
Marinobacter nauticus
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
Marinobacter nauticus 617
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced acceptor
nitrogen + H2O + acceptor
-
-
-
-
?
nitrous oxide + reduced methyl viologen
nitrogen + H2O + methyl viologen
-
-
-
?
nitrous oxide + reduced methyl viologen
nitrogen + H2O + methyl viologen
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ca2+
-
two calcium sites located at the intermonomeric surface
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
Ca2+
-
1.2 atoms per subunit
copper
-
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
-
4 atoms per subunit
Cu
-
Cu is bound by apo NosL, a coexpressed protein which is necessary for the assembling process of nitrous oxide reductase
Cu
mu4-sulfide-bridged tetranuclear CuZ cluster
Cu
-
contains 7.1 atoms per dimer
Cu
-
7.0 atoms per dimer, needs 0.001 mM Cu2+ for full activity
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
-
4.0 atoms per subunit
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
-
wild-type 7.2 atoms per protein dimer
Cu
-
CuA can exist in two oxidation forms [Cu1.5+ - Cu1.5+] and [Cu1+ - Cu1+]
Cu
-
wild-type 10.5 atoms per protein dimer
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.
Cu
-
CuA is electron transfer center, CuZ is the catalytic center
Cu
-
8 atoms per mol enzyme
Cu
-
wild-type 9.9 atoms per protein dimer
Cu
-
2.9 atoms per subunit
Cu2+
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
contains copper
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
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Haltia, T.; Brown, K.; Tegoni, M.; Gambillau, C.; Saraste, M.; Mattila, K.; Djinovic-Carugo, K.
The crystal structure of nitrous oxide reductase from Paracoccus denitrificans at 1.6 A resolution
Biochem. J.
369
77-88
2003
Paracoccus denitrificans
brenda
Rasmussen, T.; Berks, B.C.; Butt, J.N.; Thomson, A.J.
Multiple forms of the catalytic centre, Cuz, in the enzyme nitrous oxide reductase from Paracoccus pantotrophus
Biochem. J.
364
807-815
2002
Paracoccus pantotrophus
brenda
Rasmussen, T.; Berks, B.C.; Sanders-Loehr, J.; Dooley, D.M.; Zumft, W.G.; Thomson, A.J.
The catalytic center in nitrous oxide reductase, CuZ, is a copper-sulfide cluster
Biochemistry
39
12753-12756
2000
Paracoccus pantotrophus, Pseudomonas stutzeri
brenda
Prudencio, M.; Pereira, A.S.; Tavares, P.; Besson, S.; Cabrito, I.; Brown, K.; Samyn, B.; Devreese, B.; Van Beeumen, J.; Rusnak, F.; Fauque, G.; Moura, J.J.G.; Tegoni, M.; Cambillau, C.; Moura, I.
Purification, Characterization, and Preliminary Crystallographic Study of Copper-Containing Nitrous Oxide Reductase from Pseudomonas nautica 617
Biochemistry
39
3899-3907
2000
Marinobacter nauticus, Marinobacter nauticus 617
brenda
Brown, K.; Tegoni, M.; Prudencio, M.; Pereira, A.S.; Besson, S.; Moura, J.J.; Moura, I.; Cambillau, C.
A novel type of catalytic copper cluster in nitrous oxide reductase
Nat. Struct. Biol.
7
191-195
2000
Marinobacter nauticus, Marinobacter nauticus 617
brenda
Sato, K.; Okubo, A.; Yamazaki, S.
Anaerobic purification and characterization of nitrous oxide reductase from Rhodobacter sphaeroides f. sp. denitrificans IL106
J. Biochem.
125
864-868
1999
Cereibacter sphaeroides
brenda
Sabaty, M.; Schwintner, C.; Cahors, S.; Richaud, P.; Vermeglio, A.
Nitrite and nitrous oxide reductase regulation by nitrogen oxides in Rhodobacter sphaeroides f. sp. denitrificans IL106
J. Bacteriol.
181
6028-6032
1999
Cereibacter sphaeroides
brenda
Ferretti, S.; Grossmann, J.G.; Hasnain, S.S.; Eady, R.R.; Smith, B.E.
Biochemical characterization and solution structure of nitrous oxide reductase from Alcaligenes xylosoxidans (NCIMB 11015)
Eur. J. Biochem.
259
651-659
1999
Achromobacter xylosoxidans
brenda
Sato, K.; Okubo, A.; Yamazaki, S.
Characterization of a multi-copper enzyme, nitrous oxide reductase, from Rhodobacter sphaeroides f. sp. denitrificans
J. Biochem.
124
51-54
1998
Cereibacter sphaeroides
brenda
Farrar, J.A.; Zumft, W.G.; Thomson, A.J.
CuA and CuZ are variants of the electron transfer center in nitrous oxide reductase
Proc. Natl. Acad. Sci. USA
95
9891-9896
1998
Pseudomonas stutzeri
brenda
Hole, U.H.; Vollack, K.U.; Zumft, W.G.; Eisenmann, E.; Siddiqui, R.A.; Friedrich, B.; Kroneck, P.M.H.
Characterization of the membranous denitrification enzymes nitrite reductase (cytochrome cd1) and copper-containing nitrous oxide reductase from Thiobacillus denitrificans
Arch. Microbiol.
165
55-61
1996
Thiobacillus denitrificans
brenda
Dreusch, A.; Riester, J.; Kroneck, P.M.; Zumft, W.G.
Mutation of the conserved Cys165 outside of the CuA domain destabilizes nitrous oxide reductase but maintains its catalytic activity. Evidence for disulfide bridges and a putative protein disulfide isomerase gene
Eur. J. Biochem.
237
447-453
1996
Pseudomonas stutzeri
brenda
Zhang, C.s.; Hollocher, T.C.
The reaction of reduced cytochromes c with nitrous oxide reductase of Wolinella succinogenes
Biochim. Biophys. Acta
1142
253-261
1993
Wolinella succinogenes
-
brenda
Berks, B.C.; Baratta, D.; Richardson, D.J.; Ferguson, S.J.
Purification and characterization of a nitrous oxide reductase from Thiosphaera pantotropha. Implications for the mechanism of aerobic nitrous oxide reduction
Eur. J. Biochem.
212
467-476
1993
Paracoccus pantotrophus, Paracoccus pantotrophus LMD 82.5
brenda
Jones, A.M.; Knowles, R.
Denitrification in Flexibacter canadensis
Can. J. Microbiol.
36
430-434
1990
Solitalea canadensis
-
brenda
Hulse, C.L.; Averill, B.A.
Isolation of a high specific activity pink, monomeric nitrous oxide reductase from Achromobacter cycloclastes
Biochem. Biophys. Res. Commun.
166
729-735
1990
Achromobacter cycloclastes
brenda
Bonin, P.; Gilewicz, M.; Bertrand, J.C.
Effects of oxygen on each step of denitrification on Pseudomonas nautica
Can. J. Microbiol.
35
1061-1064
1989
Marinobacter nauticus
-
brenda
Teraguchi, S.; Hollocher, T.C.
Purification and some characteristics of a cytochrome c-containing nitrous oxide reductase from Wolinella succinogenes
J. Biol. Chem.
264
1972-1979
1989
Wolinella succinogenes
brenda
Viebrock, A.; Zumft, W.G.
Molecular cloning, heterologous expression, and primary structure of the structural gene for the copper enzyme nitrous oxide reductase from denitrifying Pseudomonas stutzeri
J. Bacteriol.
170
4658-4668
1988
Pseudomonas stutzeri
brenda
Coyne, M.S.; Focht, D.D.
Nitrous oxide reduction in nodules: denitrification or N2 fixation ?
Appl. Environ. Microbiol.
53
1168-1170
1987
Rhizobium sp., Rhizobium sp. 8A55
brenda
Snyder, S.W.; Hollocher, T.G.
Purification and some characteristics of nitrous oxide reductase from Paracoccus denitrificans
J. Biol. Chem.
262
6515-6525
1987
Paracoccus denitrificans
brenda
Kucera, I.; Boublikova, P.; Dadak, V.
Amperometric assay of activity and pH-optimum of N2O-reductase of Paracoccus denitrificans
Collect. Czech. Chem. Commun.
49
2709-2712
1984
Paracoccus denitrificans
-
brenda
Michalski, W.P.; Hein, D.H.; Nicholas, D.J.D.
Purification and characterization of nitrous oxide reductase from Rhodopseudomonas sphaeroides f.sp. denitrificans
Biochim. Biophys. Acta
872
50-60
1986
Cereibacter sphaeroides
-
brenda
Coyle, C.L.; Zumft, W.G.; Kroneck, P.M.H.; Krner, H.; Jakob, W.
Nitrous oxide reductase from denitrifying Pseudomonas perfectomarina. Purification and properties of a novel multicopper enzyme
Eur. J. Biochem.
153
459-467
1985
Pseudomonas stutzeri
brenda
McEwan, A.G.; Greenfield, A.J.; Wetzstein, H.G.; Jackson, J.B.; Ferguson, S.J.
Nitrous oxide reduction by members of the family Rhodospirillaceae and the nitrous oxide reductase of Rhodopseudomonas capsulata
J. Bacteriol.
164
823-830
1985
Rhodobacter capsulatus, Cereibacter sphaeroides, Rhodopseudomonas palustris, Rhodospirillum rubrum, Rhodospirillum rubrum S1, Rhodopseudomonas palustris PW5
brenda
Snyder, S.W.; Hollocher, T.C.
Nitrous oxide reductase and the 120,000 MW copper protein of N2-producing denitrifying bacteria are different entities
Biochem. Biophys. Res. Commun.
119
588-592
1984
Paracoccus denitrificans, Pseudomonas denitrificans (nom. rej.), Pseudomonas stutzeri
brenda
Aida, T.; Hata, S.; Kusunoki, H.
Temporary low oxygen conditions for the formation of nitrate reductase and nitrous oxide reductase by denitrifying Pseudomonas sp. G59
Can. J. Microbiol.
32
543-547
1986
Pseudomonas sp., Pseudomonas sp. G59
brenda
Zumft, W.G.; Matsubara, T.
A novel kind of multi-copper protein as terminal oxidoreductase of nitrous oxide respiration in Pseudomonas perfectomarinus
FEBS Lett.
148
107-112
1982
Pseudomonas stutzeri
-
brenda
Matsubara, T.; Zumft, W.G.
Identification of a copper protein as part of the nitrous oxide-reducing system in nitrite-respiring (denitrifying) Pseudomonads
Arch. Microbiol.
132
322-328
1982
Pseudomonas fluorescens
-
brenda
Kristjansson, J.K.; Hollocher, T.C.
Partial purification and characterization of nitrous oxide reductase from Paracoccus denitrificans
Curr. Microbiol.
6
247-251
1981
Paracoccus denitrificans
-
brenda
Kristjansson, J.K.; Hollocher, T.C.
First practical assay for soluble nitrous oxide reductase of denitrifying bacteria and a partial kinetic characterization
J. Biol. Chem.
255
704-707
1980
Paracoccus denitrificans
brenda
Velasco, L.; Mesa, S.; Xu, C.A.; Delgado, M.J.; Bedmar, E.J.
Molecular characterization of nosRZDFYLX genes coding for denitrifying nitrous oxide reductase of Bradyrhizobium japonicum
Antonie van Leeuwenhoek
85
229-235
2004
Bradyrhizobium japonicum (Q89XJ6), Bradyrhizobium japonicum
brenda
Chan, J.M.; Bollinger, J.A.; Grewell, C.L.; Dooley, D.M.
Reductively activated nitrous oxide reductase reacts directly with Substrate
J. Am. Chem. Soc.
126
3030-3031
2004
Achromobacter cycloclastes
brenda
Yamaguchi, K.; Kawamura, A.; Ogawa, H.; Suzuki, S.
Characterization of nitrous oxide reductase from a methylotrophic denitrifying bacterium, Hyphomicrobium denitrificans A3151
J. Biochem.
134
853-858
2003
Hyphomicrobium denitrificans, Hyphomicrobium denitrificans A3151
brenda
Arai, H.; Mizutani, M.; Igarashi, Y.
Transcriptional regulation of the nos genes for nitrous oxide reductase in Pseudomonas aeruginosa
Microbiology
149
29-36
2003
Pseudomonas aeruginosa
brenda
Mattila, K.; Haltia, T.
How does nitrous oxide reductase interact with its electron donors?--A docking study
Proteins
59
708-722
2005
Cereibacter sphaeroides, Paracoccus denitrificans (Q51705)
brenda
SooHoo, C.K.; Hollocher, T.C.
Purification and characterization of nitrous oxide reductase from Pseudomonas aeruginosa strain P2
J. Biol. Chem.
266
2203-2209
1991
Pseudomonas aeruginosa, Pseudomonas aeruginosa P2
brenda
Horn, M.A.; Drake, H.L.; Schramm, A.
Nitrous oxide reductase genes (nosZ) of denitrifying microbial populations in soil and the earthworm gut are phylogenetically similar
Appl. Environ. Microbiol.
72
1019-1026
2006
Pseudomonas sp., Dechloromonas denitrificans, Flavobacterium denitrificans, Pseudomonas sp. ED3
brenda
Sameshima-Saito, R.; Chiba, K.; Hirayama, J.; Itakura, M.; Mitsui, H.; Eda, S.; Minamisawa, K.
Symbiotic Bradyrhizobium japonicum reduces N2O surrounding the soybean root system via nitrous oxide reductase
Appl. Environ. Microbiol.
72
2526-2532
2006
Bradyrhizobium japonicum, Bradyrhizobium japonicum USDA 110
brenda
Henry, S.; Bru, D.; Stres, B.; Hallet, S.; Philippot, L.
Quantitative detection of the nosZ gene, encoding nitrous oxide reductase, and comparison of the abundances of 16S rRNA, narG, nirK, and nosZ genes in soils
Appl. Environ. Microbiol.
72
5181-5189
2006
Achromobacter cycloclastes, Alcaligenes faecalis, Bradyrhizobium japonicum, Pseudomonas denitrificans (nom. rej.), Sinorhizobium meliloti, Hyphomicrobium denitrificans, Ensifer adhaerens, Pseudomonas fluorescens (Q9F0W4), Pseudomonas denitrificans (nom. rej.) CCUG 2519, Pseudomonas fluorescens C7R12 (Q9F0W4), Sinorhizobium meliloti 50, Ensifer adhaerens SN611
brenda
Taubner, L.M.; McGuirl, M.A.; Dooley, D.M.; Copie, V.
Structural studies of Apo NosL, an accessory protein of the nitrous oxide reductase system: insights from structural homology with MerB, a mercury resistance protein
Biochemistry
45
12240-12252
2006
Achromobacter cycloclastes
brenda
Rasmussen, T.; Brittain, T.; Berks, B.C.; Watmough, N.J.; Thomson, A.J.
Formation of a cytochrome c-nitrous oxide reductase complex is obligatory for N2O reduction by Paracoccus pantotrophus
Dalton Trans.
2005
3501-3506
2005
Paracoccus pantotrophus
brenda
Wunsch, P.; Koerner, H.; Neese, F.; van Spanning, R.J.; Kroneck, P.M.; Zumft, W.G.
NosX function connects to nitrous oxide (N2O) reduction by affecting the Cu(Z) center of NosZ and its activity in vivo
FEBS Lett.
579
4605-4609
2005
Paracoccus denitrificans
brenda
Gorelsky, S.I.; Ghosh, S.; Solomon, E.I.
Mechanism of N2O reduction by the mu4-S tetranuclear CuZ cluster of nitrous oxide reductase
J. Am. Chem. Soc.
128
278-290
2006
Pseudomonas sp.
brenda
Paraskevopoulos, K.; Antonyuk, S.V.; Sawers, R.G.; Eady, R.R.; Hasnain, S.S.
Insight into catalysis of nitrous oxide reductase from high-resolution structures of resting and inhibitor-bound enzyme from Achromobacter cycloclastes
J. Mol. Biol.
362
55-65
2006
Achromobacter cycloclastes (P94127), Achromobacter cycloclastes, Achromobacter cycloclastes 1013 (P94127)
brenda
Fujita, K.; Dooley, D.M.
Insights into the mechanism of N2O reduction by reductively activated N2O reductase from kinetics and spectroscopic studies of pH effects
Inorg. Chem.
46
613-615
2007
Achromobacter cycloclastes (P94127), Achromobacter cycloclastes
brenda
Ghosh, S.; Gorelsky, S.I.; George, S.D.; Chan, J.M.; Cabrito, I.; Dooley, D.M.; Moura, J.J.; Moura, I.; Solomon, E.I.
Spectroscopic, computational, and kinetic studies of the mu4-sulfide-bridged tetranuclear CuZ cluster in N2O reductase: pH effect on the edge ligand and its contribution to reactivity
J. Am. Chem. Soc.
129
3955-3965
2007
Achromobacter cycloclastes (P94127), Achromobacter cycloclastes, Marinobacter nauticus (Q19Q69)
brenda
Fujita, K.; Chan, J.M.; Bollinger, J.A.; Alvarez, M.L.; Dooley, D.M.
Anaerobic purification, characterization and preliminary mechanistic study of recombinant nitrous oxide reductase from Achromobacter cycloclastes
J. Inorg. Biochem.
101
1836-1844
2007
Achromobacter cycloclastes (P94127), Achromobacter cycloclastes, Achromobacter cycloclastes IAM1013 (P94127)
brenda
Bingham, S.J.; Rasmussen, T.; Farrar, J.; Wolverson, D.; Thomson, A.J.
Magnetic circular dichroism anisotropy of the CuA centre of nitrous oxide reductase from coherent Raman detected electron spin resonance spectroscopy
Mol. Phys.
105
2169-2176
2007
Paracoccus pantotrophus
-
brenda
Savelieff, M.G.; Wilson, T.D.; Elias, Y.; Nilges, M.J.; Garner, D.K.; Lu, Y.
Experimental evidence for a link among cupredoxins: red, blue, and purple copper transformations in nitrous oxide reductase
Proc. Natl. Acad. Sci. USA
105
7919-7924
2008
Paracoccus denitrificans (Q51705), Paracoccus denitrificans
brenda
Fernandes, A.T.; Damas, J.M.; Todorovic, S.; Huber, R.; Baratto, M.C.; Pogni, R.; Soares, C.M.; Martins, L.O.
The multicopper oxidase from the archaeon Pyrobaculum aerophilum shows nitrous oxide reductase activity
FEBS J.
277
3176-3189
2010
Pyrobaculum aerophilum
brenda
Ertem, M.Z.; Cramer, C.J.; Himo, F.; Siegbahn, P.E.
N-O bond cleavage mechanism(s) in nitrous oxide reductase
J. Biol. Inorg. Chem.
17
687-698
2012
Paracoccus denitrificans (Q51705)
brenda
Fujita, K.; Hirasawa-Fujita, M.; Brown, D.E.; Obara, Y.; Ijima, F.; Kohzuma, T.; Dooley, D.M.
Direct electron transfer from pseudoazurin to nitrous oxide reductase in catalytic N2O reduction
J. Inorg. Biochem.
115
163-173
2012
Achromobacter cycloclastes (P94127), Achromobacter cycloclastes
brenda
DellAcqua, S.; Pauleta, S.; Moura, J.; Moura, I.
Biochemical characterization of the purple form of Marinobacter hydrocarbonoclasticus nitrous oxide reductase
Philos. Trans. R. Soc. Lond. B Biol. Sci.
367
1204-1212
2012
Marinobacter nauticus
brenda
Wan, S.; Mottiar, Y.; Johnson, A.M.; Goto, K.; Altosaar, I.
Expression of the nos operon proteins from Pseudomonas stutzeri in transgenic plants to assemble nitrous oxide reductase
Transgenic Res.
21
593-603
2012
Pseudomonas stutzeri (P19573), Pseudomonas stutzeri, Pseudomonas stutzeri ATCC 14405 (P19573)
brenda
Wyman, M.; Hodgson, S.; Bird, C.
Denitrifying alphaproteobacteria from the Arabian Sea that express nosZ, the gene encoding nitrous oxide reductase, in oxic and suboxic waters
Appl. Environ. Microbiol.
79
2670-2681
2013
Trichodesmium erythraeum, alpha proteobacterium 4N (H9A6G9), uncultured Alphaproteobacteria bacterium (M1QGM4), Trichodesmium erythraeum IMS01
brenda
Zhang, L.; Zeng, G.; Zhang, J.; Chen, Y.; Yu, M.; Lu, L.; Li, H.; Zhu, Y.; Yuan, Y.; Huang, A.; He, L.
Response of denitrifying genes coding for nitrite (nirK or nirS) and nitrous oxide (nosZ) reductases to different physico-chemical parameters during agricultural waste composting
Appl. Microbiol. Biotechnol.
99
4059-4070
2015
uncultured bacterium
brenda
Schneider, L.K.; Einsle, O.
Role of calcium in secondary structure stabilization during maturation of nitrous oxide reductase
Biochemistry
55
1433-1440
2016
Shewanella denitrificans (Q12M27), Shewanella denitrificans, Shewanella denitrificans OS217 (Q12M27)
brenda
Johnston, E.M.; DellAcqua, S.; Pauleta, S.R.; Moura, I.; Solomon, E.I.
Protonation state of the Cu4S2 CuZ site in nitrous oxide reductase redox dependence and insight into reactivity
Chem. Sci.
6
5670-5679
2015
Paracoccus pantotrophus, Pseudomonas stutzeri
brenda
Qu, Z.; Bakken, L.R.; Molstad, L.; Frostegard, A.; Bergaust, L.L.
Transcriptional and metabolic regulation of denitrification in Paracoccus denitrificans allows low but significant activity of nitrous oxide reductase under oxic conditions
Environ. Microbiol.
18
2951-2963
2016
Paracoccus denitrificans
brenda
Sanchez, C.; Mitsui, H.; Minamisawa, K.
Regulation of nitrous oxide reductase genes by NasT-mediated transcription antitermination in Bradyrhizobium diazoefficiens
Environ. Microbiol. Rep.
9
389-396
2017
Bradyrhizobium diazoefficiens (Q89XJ6), Bradyrhizobium diazoefficiens
brenda
Johnston, E.M.; Carreira, C.; DellAcqua, S.; Dey, S.G.; Pauleta, S.R.; Moura, I.; Solomon, E.I.
Spectroscopic definition of the CuZ* intermediate in turnover of nitrous oxide reductase and molecular insight into the catalytic mechanism
J. Am. Chem. Soc.
139
4462-4476
2017
Marinobacter nauticus (Q19Q69), Marinobacter nauticus 617 (Q19Q69)
brenda
Park, D.; Kim, H.; Yoon, S.
Nitrous oxide reduction by an obligate aerobic bacterium, Gemmatimonas aurantiaca strain T-27
Appl. Environ. Microbiol.
83
e00502-17
2017
Gemmatimonas aurantiaca, Gemmatimonas aurantiaca T-27
brenda
Bagherzadeh, S.; Mankad, N.P.
Oxidation of a [Cu2S] complex by N2O and CO2 insights into a role of tetranuclearity in the CuZ site of nitrous oxide reductase
Chem. Commun. (Camb.)
54
1097-1100
2018
uncultured bacterium
brenda
Zhang, L.; Bill, E.; Kroneck, P.M.H.; Einsle, O.
Histidine-gated proton-coupled electron transfer to the CuA site of nitrous oxide reductase
J. Am. Chem. Soc.
143
830-838
2021
Stutzerimonas stutzeri (P19573)
brenda
Kroneck, P.M.H.
Walking the seven lines binuclear copper A in cytochrome c oxidase and nitrous oxide reductase
J. Biol. Inorg. Chem.
23
27-39
2018
Stutzerimonas stutzeri (P19573)
brenda
Carreira, C.; Nunes, R.F.; Mestre, O.; Moura, I.; Pauleta, S.R.
The effect of pH on Marinobacter hydrocarbonoclasticus denitrification pathway and nitrous oxide reductase
J. Biol. Inorg. Chem.
25
927-940
2020
Marinobacter nauticus
brenda
Carreira, C.; Pauleta, S.R.; Moura, I.
The catalytic cycle of nitrous oxide reductase - The enzyme that catalyzes the last step of denitrification
J. Inorg. Biochem.
177
423-434
2017
Stutzerimonas stutzeri (P19573), Paracoccus denitrificans (Q51705)
brenda
Pauleta, S.R.; Carepo, M.S.P.; Moura, I.
The tetranuclear copper-sulfide center of nitrous oxide reductase
Met. Ions Life Sci.
20
139-164
2020
Wolinella succinogenes, Stutzerimonas stutzeri (P19573), Paracoccus denitrificans (Q51705), Wolinella succinogenes DSM 1740, Paracoccus denitrificans Pd1222 (Q51705)
brenda