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C551-O2 oxidoreductase
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cd1 nitrite reductase
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copper-containing dissimilatory nitrite reductase
copper-containing nitrite reductase
cytochrome c-551:O2, NO2- oxidoreductase
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cytochrome cd1 nitrite reductase
cytochrome oxidase
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dissimilatory nitrite reductase
dissimilatory nitrite reductase cytochrome cd1
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EC 1.6.6.5
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formerly
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EC 1.7.99.3
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formerly
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mitochondrial amidoxime reducing component
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oxidase, Pseudomonas cytochrome
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Pseudomonas cytochrome oxidase
reductase, nitrite (cytochrome)
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AcNIR

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AfNiR

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cd1NiR

Marinobacter nauticus
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copper-containing dissimilatory nitrite reductase

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copper-containing dissimilatory nitrite reductase
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copper-containing nitrite reductase

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copper-containing nitrite reductase
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copper-containing nitrite reductase
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copper-containing nitrite reductase
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copper-containing nitrite reductase
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copper-containing nitrite reductase
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copper-containing nitrite reductase
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copper-containing nitrite reductase
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copper-containing nitrite reductase
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copper-containing nitrite reductase
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copper-containing nitrite reductase
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copper-containing nitrite reductase
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copper-containing nitrite reductase
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copper-containing nitrite reductase
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copper-containing nitrite reductase
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copper-containing nitrite reductase
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copper-containing nitrite reductase
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copper-containing nitrite reductase
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copper-containing nitrite reductase
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copper-containing nitrite reductase
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copper-containing nitrite reductase
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copper-containing nitrite reductase
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copper-containing nitrite reductase
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copper-containing nitrite reductase
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Cu-NirK

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CuNIR

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cytochrome cd

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cytochrome cd1 nitrite reductase

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cytochrome cd1 nitrite reductase
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cytochrome cd1 nitrite reductase
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cytochrome cd1 nitrite reductase
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cytochrome cd1 nitrite reductase
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cytochrome cd1 nitrite reductase
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dissimilatory nitrite reductase

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dissimilatory nitrite reductase
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dissimilatory nitrite reductase
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GtNiR

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HdNIR

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HYPDE_25578

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MRA2164

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NiR

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NiR-Pa

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NirK

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NirS

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nitrite reductase

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PNR

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Pseudomonas cytochrome oxidase

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Pseudomonas cytochrome oxidase
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Rpic_4015

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S58_68210

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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
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nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
electron transfer from c heme to d1 heme is very slow, order of seconds
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nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
electron-transfer mechanism
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nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
rate constants of intermolecular electron transfer
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nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
proposed reaction mechanism
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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
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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
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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
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nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
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nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
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nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
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nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
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nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
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nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
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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
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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
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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
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?
N,N-dimethyl-p-phenylenediamine + oxidized benzyl viologen
?
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?
NH2OH + NaNO2
N2O + H2O
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?
NH2OH + reduced cytochrome c550
NH3 + H2O + oxidized cytochrome c550
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additional electron donor: horse heart cytochrome c
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?
nitric oxide + H2O + ferricytochrome c
nitrite + ferrocytochrome c + 2 H+
Marinobacter nauticus
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?
nitric oxide + H2O + ferricytochrome c
nitrite + ferrocytochrome c + H+
nitric oxide + H2O + ferricytochrome c B0428
nitrite + ferrocytochrome c B0428 + 2 H+
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?
nitric oxide + H2O + ferricytochrome c551
nitrite + ferrocytochrome c551 + 2 H+
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?
nitric oxide + H2O + ferricytochrome c551
nitrite + ferrocytochrome c551 + H+
nitric oxide + H2O + ferricytochrome c552
nitrite + ferrocytochrome c552 + 2 H+
Marinobacter nauticus
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?
nitric oxide + H2O + oxidized phenazine methosulfate
nitrite + reduced phenazine methosulfate + 2 H+
Marinobacter nauticus
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phenazine methosulfate can serve as reducing agents and trigger catalytic activity if the assay is performed in relatively long time windows
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?
nitric oxide + H2O + oxidized phenosafranin
nitrite + reduced phenosafranin + 2 H+
Marinobacter nauticus
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phenosafranin can serve as reducing agents and trigger catalytic activity if the assay is performed in relatively long time windows
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?
nitrite + dithionite
NO + reduced dithionite
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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
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?
nitrite + electron donor
NO + oxidized electron donor
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?
nitrite + electron donor
NO + oxidized electron donor + H2O
nitrite + ferrocytochrome b5 + 2 H+
nitric oxide + H2O + ferricytochrome b5
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?
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)
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?
nitrite + ferrocytochrome c2
NO + H2O + ferricytochrome c2
nitrite + ferrocytochrome c550
NO + ferricytochrome c550
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?
nitrite + ferrocytochrome c550
NO + oxidized ferricytochrome c550
nitrite + ferrocytochrome V(gamma) + H+
nitric oxide + H2O + ferricytochrome V(gamma)
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r
nitrite + H2O + reduced cytochrome cd1
nitric oxide + H+ + cytochrome cd1
anaerobic assay conditions
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?
nitrite + H2O + reduced pseudoazurin
nitric oxide + H+ + pseudoazurin
nitrite + methyl viologen
NO + oxidized methyl viologen + H2O
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?
nitrite + reduced ascorbate
nitric oxide + oxidized ascorbate
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r
nitrite + reduced azurin
NO + H2O + oxidized azurin
nitrite + reduced azurin
NO + oxidized azurin
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azurin purified from Pseudomonas chlororaphis
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?
nitrite + reduced azurin I
NO + azurin I
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?
nitrite + reduced azurin I
NO + oxidized azurin I
nitrite + reduced benzyl viologen
nitric oxide + oxidized benzyl viologen
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?
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
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random sequential mechanism
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?
nitrite + reduced methyl viologen
NO + oxidized methyl viologen + H2O
nitrite + reduced phenazine methosulfate
NO + oxidized phenazine methosulfate
nitrite + reduced pseudoazurin
NO + H2O + oxidized pseudoazurin
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-
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?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
nitrite + reduced pseudoazurin + H+
nitric oxide + oxidized pseudoazurin + H2O
NO2 + reduced methyl viologen
NO + oxidized methylviologen
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?
NO2- + ferrocytochrome c
NO + ferricytochrome c
NO2- + morpholine
N-nitrosomorpholine
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in the presence of diethyldithiocarbamic acid ethylester, nitrosation through the production of NO or NO+-like species
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?
NO2- + Na2S2O4
NO + Na2S2O3
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pysiological electron donor is unknown, no activity with methyl viologen, phenazine methosulfate or N,N,N',N',-tetramethyl-p-phenylenediamine
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?
NO2- + reduced ascorbate
NO + oxidized ascorbate
NO2- + reduced azurin
NO + oxidized azurin
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putative physiological electron donor
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?
NO2- + reduced cytochrome c550
NO + oxidized cytochrome c550
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unambiguously identified as physiological electron donor
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?
NO2- + reduced pseudoazurin
NO + oxidized pseudoazurin
O2 + ferrocytochrome c
H2O + ferricytochrome c