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nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+

proposed reaction mechanism
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
electron-transfer mechanism
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
electron transfer from c heme to d1 heme is very slow, order of seconds
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
rate constants of intermolecular electron transfer
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
a copper protein, cytochrome c-552 or cytochrome c-553 from Pseudomonas denitrificans acts as acceptor
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
mechanism
-
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+
reaction mechanism, overview. The transformation from the initial O-coordination of substrate to the final N-coordination of product is achieved by electron transfer from T1 copper to T2 copper, rather than by the previously reported side-on coordination of a NO intermediate, which only takes place in the reduced enzyme. Role of structural change in the critical residue Asp98, which affects the energetics of substrate attachment and product release at the T2 copper reaction center, while it does not significantly affect the activation energy and reaction pathways of the nitrite reduction process
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
the proposed mechanisms for the reduction of nitrite by CuNiRs include intramolecular electron and proton transfers, proton-coupled electron transfer is one of the key processes in enzyme reactions, density functional theory calculations analysis. The reduction of T2 Cu site promotes the proton transfer, and the hydrogen bond network around the binding site has an important role not only to stabilize the nitrite binding but also to promote the proton transfer to nitrite. Reaction mechanism, overview
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
I7ESA1;
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
I3X948;
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
reaction mechanism, overview. Mobility of two residues essential to catalytic activity, Asp98 and His244, are sterically restricted in GtNIR by Phe109 on a characteristic loop structure that is found above Asp98 and by an unusually short CH-O hydrogen bond observed between His244 and water, respectively. Analysis of the hydrogen-bond networks around His244 and the flow path of protons consumed by nitrite reduction. The electron transfer reaction is coupled with the proton transfer reaction
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
-
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
-
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
reaction mechanism, overview. Mobility of two residues essential to catalytic activity, Asp98 and His244, are sterically restricted in GtNIR by Phe109 on a characteristic loop structure that is found above Asp98 and by an unusually short CH-O hydrogen bond observed between His244 and water, respectively. Analysis of the hydrogen-bond networks around His244 and the flow path of protons consumed by nitrite reduction. The electron transfer reaction is coupled with the proton transfer reaction; the proposed mechanisms for the reduction of nitrite by CuNiRs include intramolecular electron and proton transfers, proton-coupled electron transfer is one of the key processes in enzyme reactions, density functional theory calculations analysis. The reduction of T2 Cu site promotes the proton transfer, and the hydrogen bond network around the binding site has an important role not only to stabilize the nitrite binding but also to promote the proton transfer to nitrite. Reaction mechanism, overview
-
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
-
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
-
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
-
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
-
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
catalytic mechansim, overview
-
-
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
-
-
-
-
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evolution

the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
I7ESA1;
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
I3X948;
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
evolution
-
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
-
evolution
-
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
-
evolution
-
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
-
evolution
-
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
-
evolution
-
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
-
evolution
-
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
-
evolution
-
the copper-containing nitrite reductase is observed in mostly gram negative denitrifying soil bacteria. The microorganisms containing the copper-containing nitrite reductase are typically found in the low oxygen containing environments
-
metabolism

-
the enzyme is involved in the denitrification anoxic process, which occurs in four reduction steps: initial conversion of nitrate to nitrite, followed by transformation of nitrite to nitric oxide, subsequent reduction of nitric oxide to nitrous oxide, and the final conversion of nitrous oxide to dinitrogen gas. All stages are catalyzed by complex metalloenzymes with different transition metal cofactors. Dissimilatory nitrite reductases (NiRs) catalyze the reduction of nitrite to nitric oxide, the committed step in denitrification. There are two main types: one containing iron (cd1NiRs) and the other copper (CuNiRs)
metabolism
-
the enzyme catalyzes the key reaction in denitrification as the nitrogen compound is changed from an ionic state to a gaseous molecule
metabolism
-
the enzyme catalyzes the key reaction in denitrification as the nitrogen compound is changed from an ionic state to a gaseous molecule
-
physiological function

deletion of cytochrome cd1-type nitrite reductase NirS gene or gene NirN results in impaired growth and smaller, fewer, and aberrantly shaped magnetite crystals during nitrate reduction. Nitrite reduction is completely abolished in the DELTAnirS mutant. NirN is required for full reductase activity of NirS by maintaining a proper form of d1 heme for holo-cytochrome cd1 assembly
physiological function
-
dissimilatory reduction of nitrite by copper-containing nitrite reductase (CuNiR) is an important step in the geobiochemical nitrogen cycle
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
I7ESA1;
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
I3X948;
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
physiological function
-
copper-containing nitrite reductase (CuNIR) catalyzes the reduction of nitrite (NO2 ) to nitric oxide (NO) during denitrification
physiological function
-
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
-
physiological function
-
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
-
physiological function
-
copper-containing nitrite reductase (CuNIR) catalyzes the reduction of nitrite (NO2 ) to nitric oxide (NO) during denitrification; dissimilatory reduction of nitrite by copper-containing nitrite reductase (CuNiR) is an important step in the geobiochemical nitrogen cycle
-
physiological function
-
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
-
physiological function
-
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
-
physiological function
-
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
-
physiological function
-
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
-
physiological function
-
Nirk is a copper-containing nitrite reductase (CuNiR) and a key catalytic enzyme in the environmental denitrification process that helps to produce nitric oxide from nitrite, molecular mechanism of denitrification process, overview
-
additional information

-
determination of the activation energies, transition states, and minimum energy pathways of CuNiR for reaction mechanism analysis. Structure modelling of the CuNiR active site involving residues His100, His135, His306, Asp98, His255, Ile257 and four water molecules. Structure-function analysis, detailed overview
additional information
-
geometric structure of the nitrite-bound T2 Cu site in GtNiR using density functional theory, DFT, calculations. The reduction of T2 Cu site promotes the proton transfer. Optimized structures of nitrite binding forms under physiological pH conditions and in neutral states, detailed overview
additional information
-
geometric structure of the nitrite-bound T2 Cu site in GtNiR using density functional theory, DFT, calculations. The reduction of T2 Cu site promotes the proton transfer. Optimized structures of nitrite binding forms under physiological pH conditions and in neutral states, detailed overview
-
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ferrocytochrome c + O2
ferricytochrome c + H2O
ferrocytochrome c-551 + NO2-
NO + ferricytochrome c-551
ferrocytochrome c-551 + O2
ferricytochrome c-551 + H2O
ferrocytochrome c-551 + O2
H2O + ferricytochrome c-551
hydroxylamine + reduced pseudoazurin
NH3 + H2O + oxidized pseudoazurin
-
-
-
-
?
N,N-dimethyl-p-phenylenediamine + oxidized benzyl viologen
?
-
-
-
-
?
NH2OH + NaNO2
N2O + H2O
-
-
-
?
NH2OH + reduced cytochrome c550
NH3 + H2O + oxidized cytochrome c550
-
additional electron donor: horse heart cytochrome c
-
?
nitric oxide + H2O + ferricytochrome c
nitrite + ferrocytochrome c + 2 H+
-
-
-
-
?
nitric oxide + H2O + ferricytochrome c551
nitrite + ferrocytochrome c551 + 2 H+
-
-
-
?
nitric oxide + H2O + ferricytochrome c552
nitrite + ferrocytochrome c552 + 2 H+
-
-
-
-
?
nitric oxide + H2O + oxidized phenazine methosulfate
nitrite + reduced phenazine methosulfate + 2 H+
-
phenazine methosulfate can serve as reducing agents and trigger catalytic activity if the assay is performed in relatively long time windows
-
-
?
nitric oxide + H2O + oxidized phenosafranin
nitrite + reduced phenosafranin + 2 H+
-
phenosafranin can serve as reducing agents and trigger catalytic activity if the assay is performed in relatively long time windows
-
-
?
nitrite + dithionite
NO + reduced dithionite
-
type 1 copper of the fully loaded protein is reduced both directly by dithionite and indirectly by the type 2 copper site via intramolecular electron transfer
-
-
?
nitrite + electron donor
NO + oxidized electron donor
-
-
-
-
?
nitrite + electron donor
NO + oxidized electron donor + H2O
nitrite + ferrocytochrome b5 + 2 H+
nitric oxide + H2O + ferricytochrome b5
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
nitrite + ferrocytochrome c(gamma)
NO + H2O + ferricytochrome c(gamma)
nitrite + ferrocytochrome c2
NO + H2O + ferricytochrome c2
nitrite + ferrocytochrome c550
NO + ferricytochrome c550
-
-
-
-
?
nitrite + ferrocytochrome c550
NO + oxidized ferricytochrome c550
nitrite + H2O + reduced cytochrome cd1
nitric oxide + H+ + cytochrome cd1
-
anaerobic assay conditions
-
-
?
nitrite + H2O + reduced pseudoazurin
nitric oxide + H+ + pseudoazurin
nitrite + methyl viologen
NO + oxidized methyl viologen + H2O
A9XR52;
-
-
-
?
nitrite + reduced azurin
NO + H2O + oxidized azurin
nitrite + reduced azurin
NO + oxidized azurin
-
azurin purified from Pseudomonas chlororaphis
-
-
?
nitrite + reduced azurin I
NO + azurin I
-
-
-
?
nitrite + reduced azurin I
NO + oxidized azurin I
nitrite + reduced benzyl viologen
nitric oxide + oxidized benzyl viologen
-
-
-
-
?
nitrite + reduced benzyl viologen
NO + H2O + oxidized benzyl viologen
nitrite + reduced benzyl viologen
NO + oxidized benzyl viologen
nitrite + reduced electron donor
NO + H2O + oxidized electron donor
nitrite + reduced hydroquinone
nitric oxide + H2O + hydroquinone
nitrite + reduced methyl viologen
NO + oxidized methyl viologen
-
random sequential mechanism
-
-
?
nitrite + reduced methyl viologen
NO + oxidized methyl viologen + H2O
nitrite + reduced pseudoazurin
NO + H2O + oxidized pseudoazurin
-
-
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
NO2 + reduced methyl viologen
NO + oxidized methylviologen
-
-
-
?
NO2- + ferrocytochrome c
NO + ferricytochrome c
NO2- + morpholine
N-nitrosomorpholine
-
in the presence of diethyldithiocarbamic acid ethylester, nitrosation through the production of NO or NO+-like species
-
?
NO2- + Na2S2O4
NO + Na2S2O3
-
pysiological electron donor is unknown, no activity with methyl viologen, phenazine methosulfate or N,N,N',N',-tetramethyl-p-phenylenediamine
-
?
NO2- + reduced ascorbate
NO + oxidized ascorbate
NO2- + reduced azurin
NO + oxidized azurin
-
putative physiological electron donor
-
?
NO2- + reduced cytochrome c550
NO + oxidized cytochrome c550
-
unambiguously identified as physiological electron donor
-
?
NO2- + reduced pseudoazurin
NO + oxidized pseudoazurin
O2 + ferrocytochrome c
H2O + ferricytochrome c
O2 + reduced pseudoazurin
H2O + oxidized pseudoazurin
-
-
-
-
?
O2-. + H+
H2O2 + O2
-
purified enzyme shows superoxide dismutase activity, approx. one-third that of pure superoxide dismutase
-
-
reduced azurin + O2
oxidized azurin + H2O
reduced tetramethyl-4-phenylenediamine + NO2
oxidized tetrametyl-4-phenylenediamine + NO
-
no reaction with horse ferrocytochrome c, Neurospora europaea ferrocytochrome c-552, Magnetospirillum magnetotacticum ferrocytochrome c-550 and Pseudomonas aeruginosa cytochrome c-551
-
?
reduced tetramethyl-4-phenylenediamine + O2
oxidized tetrametyl-4-phenylenediamine + H2O
-
-
-
?
additional information
?
-
ferrocytochrome c + O2

ferricytochrome c + H2O
-
-
-
?
ferrocytochrome c + O2
ferricytochrome c + H2O
-
in the presence of ascorbate, N,N,N',N-tetramethyl-p-phenylenediamine and cytochrome c-553
-
?
ferrocytochrome c-551 + NO2-

NO + ferricytochrome c-551
-
-
-
?
ferrocytochrome c-551 + NO2-
NO + ferricytochrome c-551
-
-
-
-
ferrocytochrome c-551 + NO2-
NO + ferricytochrome c-551
-
-
-
-
ferrocytochrome c-551 + O2

ferricytochrome c-551 + H2O
-
-
-
-
ferrocytochrome c-551 + O2
ferricytochrome c-551 + H2O
-
-
-
?
ferrocytochrome c-551 + O2
ferricytochrome c-551 + H2O
-
-
-
-
?
ferrocytochrome c-551 + O2

H2O + ferricytochrome c-551
-
-
-
?
ferrocytochrome c-551 + O2
H2O + ferricytochrome c-551
-
-
-
-
ferrocytochrome c-551 + O2
H2O + ferricytochrome c-551
-
also reacts with horse heart cytochrome c
-
-
ferrocytochrome c-551 + O2
H2O + ferricytochrome c-551
-
-
-
-
ferrocytochrome c-551 + O2
H2O + ferricytochrome c-551
-
-
-
?
ferrocytochrome c-551 + O2
H2O + ferricytochrome c-551
-
-
-
-
?
ferrocytochrome c-551 + O2
H2O + ferricytochrome c-551
-
inactive with eukaryotic cytochromes c
-
-
nitrite + electron donor

NO + oxidized electron donor + H2O
-
mitochondrial electron carrier cytochrome c can also effectively reduce nitrite to NO. This nitrite reductase activity is highly regulated as it is dependent on pentacoordination of the heme iron in the protein and occurs under anoxic and acidic conditions. In the presence of nitrite, pentacoordinate cytochrome c generates bioavailable NO that is able to inhibit mitochondrial respiration
-
-
?
nitrite + electron donor
NO + oxidized electron donor + H2O
-
-
-
?
nitrite + ferrocytochrome c

nitric oxide + H2O + ferricytochrome c
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
artificial electron donors: reduced methyl viologen, phenazine methosulfate and to a lesser extend hydroquinone, highly purified enzyme has cytochrome c oxidase activity
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
artificial electron donor: reduced benzyl viologen
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
artificial electron donors: thionine, brilliant cresyl blue, methylene blue, 2,6-dichlorophenolindophenol or Pseudomonas stutzeri cytochrome c-552 and 558
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c
nitric oxide + H2O + ferricytochrome c
-
artificial electron donor: reduced benzyl viologen
-
?
nitrite + ferrocytochrome c

NO + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c + 2 H+

nitric oxide + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
I7ESA1;
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
I7ESA1;
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
I3X948;
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
I3X948;
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
?
nitrite + ferrocytochrome c(gamma)

NO + H2O + ferricytochrome c(gamma)
-
-
-
-
?
nitrite + ferrocytochrome c(gamma)
NO + H2O + ferricytochrome c(gamma)
-
-
-
-
?
nitrite + ferrocytochrome c2

NO + H2O + ferricytochrome c2
-
-
-
-
?
nitrite + ferrocytochrome c2
NO + H2O + ferricytochrome c2
-
there is likely an unidentified electron donor, in addition to c2 that transfers electrons to nitrite reductase
-
-
?
nitrite + ferrocytochrome c2
NO + H2O + ferricytochrome c2
-
-
-
-
?
nitrite + ferrocytochrome c2
NO + H2O + ferricytochrome c2
-
there is likely an unidentified electron donor, in addition to c2 that transfers electrons to nitrite reductase
-
-
?
nitrite + ferrocytochrome c550

NO + oxidized ferricytochrome c550
-
-
-
-
?
nitrite + ferrocytochrome c550
NO + oxidized ferricytochrome c550
-
-
-
-
?
nitrite + H2O + reduced pseudoazurin

nitric oxide + H+ + pseudoazurin
-
reduction of pseudoazurin by ascorbate
-
-
?
nitrite + H2O + reduced pseudoazurin
nitric oxide + H+ + pseudoazurin
-
reduction of pseudoazurin by ascorbate
-
-
?
nitrite + reduced azurin

NO + H2O + oxidized azurin
-
-
-
-
?
nitrite + reduced azurin
NO + H2O + oxidized azurin
-
-
-
-
?
nitrite + reduced azurin I

NO + oxidized azurin I
-
-
-
-
?
nitrite + reduced azurin I
NO + oxidized azurin I
-
coordinate synthesis of azurin I and copper nitrite reductase in Alcaligenes xylosoxidans during denitrification
-
-
?
nitrite + reduced benzyl viologen

NO + H2O + oxidized benzyl viologen
-
-
-
-
?
nitrite + reduced benzyl viologen
NO + H2O + oxidized benzyl viologen
-
-
-
-
?
nitrite + reduced benzyl viologen
NO + H2O + oxidized benzyl viologen
-
-
-
-
?
nitrite + reduced benzyl viologen

NO + oxidized benzyl viologen
-
random sequential mechanism
-
-
?
nitrite + reduced benzyl viologen
NO + oxidized benzyl viologen
-
-
-
-
?
nitrite + reduced electron donor

NO + H2O + oxidized electron donor
-
-
-
-
?
nitrite + reduced electron donor
NO + H2O + oxidized electron donor
-
-
-
-
?
nitrite + reduced hydroquinone

nitric oxide + H2O + hydroquinone
-
-
-
?
nitrite + reduced hydroquinone
nitric oxide + H2O + hydroquinone
-
-
-
?
nitrite + reduced methyl viologen

NO + oxidized methyl viologen + H2O
-
-
-
-
?
nitrite + reduced methyl viologen
NO + oxidized methyl viologen + H2O
-
-
-
-
?
nitrite + reduced methyl viologen
NO + oxidized methyl viologen + H2O
-
-
-
?
nitrite + reduced methyl viologen
NO + oxidized methyl viologen + H2O
-
-
-
?
nitrite + reduced pseudoazurin

NO + oxidized pseudoazurin
-
the rate-determining step in the enzyme reaction sequence is not the intermolecular electron transfer process between pseudoazurin and AcNIR, but the reduction of substrate by AcNIR in the steady-state assay system
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
the rate-determining step in the enzyme reaction sequence is not the intermolecular electron transfer process between pseudoazurin and AcNIR, but the reduction of substrate by AcNIR in the steady-state assay system
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
-
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
pseudoazurin from Achromobacter cycloclastes
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
-
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
-
-
-
r
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
random sequential mechanism
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
-
-
-
r
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
-
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
cytochrome c550 and pseudoazurin are the alternative electron mediator proteins between the cytochrome bc1 and the cytochrome cd1 type nitrite reductase
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
-
-
-
?
NO2- + ferrocytochrome c

NO + ferricytochrome c
-
role in respiration
-
-
?
NO2- + ferrocytochrome c
NO + ferricytochrome c
-
probably most dominant activity in vivo
-
-
NO2- + reduced ascorbate

NO + oxidized ascorbate
-
physiological electron donor is not known, 7% activity if NADH is used as artificial electron donor
-
?
NO2- + reduced ascorbate
NO + oxidized ascorbate
-
-
-
-
NO2- + reduced pseudoazurin

NO + oxidized pseudoazurin
-
-
-
?
NO2- + reduced pseudoazurin
NO + oxidized pseudoazurin
-
unambiguously identified as physiological electron donor
-
?
O2 + ferrocytochrome c

H2O + ferricytochrome c
-
-
-
-
?
O2 + ferrocytochrome c
H2O + ferricytochrome c
-
-
-
-
?
reduced azurin + O2

oxidized azurin + H2O
-
putative physiological electron donor
-
-
?
reduced azurin + O2
oxidized azurin + H2O
-
not known whether azurin donates electrons in vivo in parallel or sequentially to cytochrome c551
-
-
additional information

?
-
-
theoretical investigation has provided a number of insights into the reaction mechanism of copper nitrite reductase: The results presented in this paper indicate that the hydroxyl-intermediate pathway appears unlikely for the main reaction. The results also indicate that Asp-92 may play a significant structural role through hydrogen-bonding to the protonated oxygen of the nitrite substrate, and thereby elongating the N O bond, which is to be cleaved
-
-
-
additional information
?
-
density functional theory study of nitrite and nitric oxide adducts
-
-
-
additional information
?
-
-
the active site residue is Ile257. The small molecules formate, acetate and nitrate mimic the substrate by having at least two oxygen atoms for bidentate coordination to the type 2 copper atom and interacting wit the oxidized catalytic metal ion, overview. Nitrite and the substrate mimic bind in the same asymmetric, bidentate manner
-
-
-
additional information
?
-
-
the active site residue is Ile257. The small molecules formate, acetate and nitrate mimic the substrate by having at least two oxygen atoms for bidentate coordination to the type 2 copper atom and interacting wit the oxidized catalytic metal ion, overview. Nitrite and the substrate mimic bind in the same asymmetric, bidentate manner
-
-
-
additional information
?
-
-
cross-linked hemoglobin bis-tetramers with good oxygen delivery potential have 3fold enhanced nitrite reductase activity, compared to native protein and cross-linked tetramers. Conjugation of four polyethylene glocol chains to the bis-tetramer at each beta-Cys-93 produces a material with additionallly 2.5fold increased nitrite reductase activity while retaining cooperativity
-
-
-
additional information
?
-
mARC can generate nitric oxide from nitrite when forming an electron transfer chain with NADH, cytochrome b5, and NADH-dependent cytochrome b5 reductase
-
-
-
additional information
?
-
mARC can generate nitric oxide from nitrite when forming an electron transfer chain with NADH, cytochrome b5, and NADH-dependent cytochrome b5 reductase
-
-
-
additional information
?
-
a conserved and functional aniA gene is not essential for meningococcal survival
-
-
-
additional information
?
-
-
simulation of the NO kinetics observed in batch cultures of Paracoccus denitrificans, including aerobic and anaerobic growth, the kinetics of O2 consumption and denitrification. The model predicts NO concentrations close to that measured. The predicted steady-state NO aqueous concentration for an actively denitrifying population is 35 nM
-
-
-
additional information
?
-
-
activity is associated with histidine/methionine coordination at heme c, and the cytochrome cd1 is activated by exposure to its physiological substrate without the necessity of passing through the reduced state
-
-
-
additional information
?
-
-
nitrite reductase from Pseudomonas aeruginosa released by antimicrobial agents and complement induces interleukin-8 production in bronchial epithelial cells
-
-
-
additional information
?
-
-
nitrite reductase in both oxidized and reduced states forms with NO two distinct compounds at both hemes. These compounds, in addition to the oxidized and reduced enzymes, are formed during the turnover of this enzyme as functional intermediates
-
-
-
additional information
?
-
-
spectroscopic analysis of the reactivity of cd1NiR and its semi-apo derivative with NO. The c heme nitrosylation is enhanced during catalysis
-
-
-
additional information
?
-
-
nitrite reductase from Pseudomonas aeruginosa released by antimicrobial agents and complement induces interleukin-8 production in bronchial epithelial cells
-
-
-
additional information
?
-
activity is associated with histidine/methionine coordination at heme c, and the cytochrome cd1 is activated by exposure to its physiological substrate without the necessity of passing through the reduced state, reactivity toward nitrite is also observed for oxidized cytochrome cd1 from Pseudomonas stutzeri suggesting a more general involvement of the EPR-silent FeIII heme d1 species in nitrite reduction
-
-
-
additional information
?
-
activity is associated with histidine/methionine coordination at heme c, and the cytochrome cd1 is activated by exposure to its physiological substrate without the necessity of passing through the reduced state, reactivity toward nitrite is also observed for oxidized cytochrome cd1 from Pseudomonas stutzeri suggesting a more general involvement of the EPR-silent FeIII heme d1 species in nitrite reduction
-
-
-
additional information
?
-
-
electrocatalytic reduction of nitrite to NO by CuMe2bpaCl2, as a model for the active site of copper containing nitrite reductase. The 77-K EPR spectrum of CuMe2bpaCl2 in the collagen matrix reveals the typical axial signals of a tetragonal Cu2+ chromophore. The redox potential is -63 mV at pH 5.5. In the presence of nitrite, an increase in the cathodic current is observed in the cyclic voltammogram of CuMe2bpaCl2 in the collagen matrix. Upon reaching -300 mV, a linear generation of NO is observed for the CuMe2bpaCl2/collagen film-coated electrode. The relationship between the rate of NO generation and the nitrite concentration in solution using the Michaelis-Menten equation, results in Vmax 3.16 nM per s and Km 1.1 mM at pH 5.5. The current increase and the reaction rate are dependent on the pH of the solution. The mechanism of nitrite reduction by the copper complex in the collagen matrix is the same mechanism as that of the enzyme in aqueous solution
-
-
-
additional information
?
-
-
study on strucuture-function relationship using copper(I)-nitrite complexes with sterically hindered tris(4-imidazolyl)carbinols such as tris(1-methyl-2-ethyl-4-imidazolyl)carbinol, tris(1-methyl-2-isopropyl-4-imidazolyl)carbinol, or tris(1-pyrazolyl)methanes such as tris(3,5-dimethyl-1-pyrazolyl)methane or tris(3,5-diethyl-1-pyrazolyl)methane, and tris(3,5-diisopropyl-1-pyrazolyl)methane. All of these complexes are good functional models of Cu-NiR that form NO and copper(II) acetate complexes well from reactions with acetic acid under anaerobic conditions. The copper(I) nitrite complex with the tris(1-methyl-2-ethyl-4-imidazolyl)carbinol ligand, which is similar to the highly conserved three-histidine (His)3 ligand environment in the catalytic site of Cu-NiR, has the highest Cu-NiR activity
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ferrocytochrome c-551 + O2
ferricytochrome c-551 + H2O
-
-
-
-
nitric oxide + H2O + ferricytochrome c552
nitrite + ferrocytochrome c552 + 2 H+
-
-
-
-
?
nitrite + electron donor
NO + oxidized electron donor
-
-
-
-
?
nitrite + electron donor
NO + oxidized electron donor + H2O
-
mitochondrial electron carrier cytochrome c can also effectively reduce nitrite to NO. This nitrite reductase activity is highly regulated as it is dependent on pentacoordination of the heme iron in the protein and occurs under anoxic and acidic conditions. In the presence of nitrite, pentacoordinate cytochrome c generates bioavailable NO that is able to inhibit mitochondrial respiration
-
-
?
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
nitrite + ferrocytochrome c2
NO + H2O + ferricytochrome c2
nitrite + ferrocytochrome c550
NO + ferricytochrome c550
-
-
-
-
?
nitrite + reduced azurin I
NO + oxidized azurin I
-
coordinate synthesis of azurin I and copper nitrite reductase in Alcaligenes xylosoxidans during denitrification
-
-
?
nitrite + reduced electron donor
NO + H2O + oxidized electron donor
nitrite + reduced pseudoazurin
NO + H2O + oxidized pseudoazurin
-
-
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
NO2- + ferrocytochrome c
NO + ferricytochrome c
NO2- + reduced cytochrome c550
NO + oxidized cytochrome c550
-
unambiguously identified as physiological electron donor
-
?
NO2- + reduced pseudoazurin
NO + oxidized pseudoazurin
-
unambiguously identified as physiological electron donor
-
?
reduced azurin + O2
oxidized azurin + H2O
additional information
?
-
nitrite + ferrocytochrome c

NO + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c
NO + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c + 2 H+

nitric oxide + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
G7ZE78
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
G7ZE78
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
A0A085FMZ3
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
M4Z2Q6
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
M4Z2Q6
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
A4IL26
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
A4IL26
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
-
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
A0A090F2L3
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
I7ESA1
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
I7ESA1
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
A0A2C9EU40
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
A0A2C9EU40
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
A0A021X0B0
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
I3X948
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
I3X948
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
A0A077M3S9
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
A0A077M3S9
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
A0A077MDD6
-
-
-
?
nitrite + ferrocytochrome c + 2 H+
nitric oxide + H2O + ferricytochrome c
A0A077MDD6
-
-
-
?
nitrite + ferrocytochrome c2

NO + H2O + ferricytochrome c2
-
there is likely an unidentified electron donor, in addition to c2 that transfers electrons to nitrite reductase
-
-
?
nitrite + ferrocytochrome c2
NO + H2O + ferricytochrome c2
-
there is likely an unidentified electron donor, in addition to c2 that transfers electrons to nitrite reductase
-
-
?
nitrite + reduced electron donor

NO + H2O + oxidized electron donor
-
-
-
-
?
nitrite + reduced electron donor
NO + H2O + oxidized electron donor
-
-
-
-
?
nitrite + reduced pseudoazurin

NO + oxidized pseudoazurin
-
-
-
-
?
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
-
-
-
r
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
-
-
-
r
nitrite + reduced pseudoazurin
NO + oxidized pseudoazurin
-
cytochrome c550 and pseudoazurin are the alternative electron mediator proteins between the cytochrome bc1 and the cytochrome cd1 type nitrite reductase
-
-
?
NO2- + ferrocytochrome c

NO + ferricytochrome c
-
role in respiration
-
-
?
NO2- + ferrocytochrome c
NO + ferricytochrome c
-
probably most dominant activity in vivo
-
-
reduced azurin + O2

oxidized azurin + H2O
-
putative physiological electron donor
-
-
?
reduced azurin + O2
oxidized azurin + H2O
-
not known whether azurin donates electrons in vivo in parallel or sequentially to cytochrome c551
-
-
additional information

?
-
-
cross-linked hemoglobin bis-tetramers with good oxygen delivery potential have 3fold enhanced nitrite reductase activity, compared to native protein and cross-linked tetramers. Conjugation of four polyethylene glocol chains to the bis-tetramer at each beta-Cys-93 produces a material with additionallly 2.5fold increased nitrite reductase activity while retaining cooperativity
-
-
-
additional information
?
-
Q9JYE1
a conserved and functional aniA gene is not essential for meningococcal survival
-
-
-
additional information
?
-
-
nitrite reductase from Pseudomonas aeruginosa released by antimicrobial agents and complement induces interleukin-8 production in bronchial epithelial cells
-
-
-
additional information
?
-
-
nitrite reductase from Pseudomonas aeruginosa released by antimicrobial agents and complement induces interleukin-8 production in bronchial epithelial cells
-
-
-
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.
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.
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0.0305 - 0.046
cytochrome c
0.00177 - 0.0075
cytochrome c551
-
0.079
ferricytochrome c551
pH 8.0, 25°C
-
0.0018 - 0.0075
Ferrocytochrome c-551
-
0.067 - 0.16
pseudoazurin
-
0.41
reduced methyl viologen
pH and temperature not specified in the publication
additional information
additional information
-
0.00084
azurin

-
recombinant Y10F mutant enzyme, at pH 6.2 and 27°C
0.035
azurin
-
recombinant wild-type and Y10F mutant enzyme, at pH 6.2 and 27°C
0.0305
cytochrome c

-
succinylated monomeric enzyme
0.00177
cytochrome c551

-
recombinant wild-type enzyme, at pH 6.2 and 27°C
-
0.0018
cytochrome c551
-
recombinant H327A mutant enzyme, O2 reduction
-
0.002
cytochrome c551
-
recombinant wild-type enzyme, O2 reduction
-
0.0056
cytochrome c551
-
also known as cytochrome c8
-
0.0075
cytochrome c551
-
recombinant H369A mutant enzyme, O2 reduction
-
0.0018
Ferrocytochrome c-551

-
pH 6.2, 25°C, mutant enzyme H327A
-
0.002
Ferrocytochrome c-551
-
pH 6.2, 25°C, wild-type enzyme
-
0.0075
Ferrocytochrome c-551
-
pH 6.2, 25°C, mutant enzyme H369A
-
0.43
hydroxylamine

-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor horse heart cytochrome c
0.68
hydroxylamine
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor cytochrome c550
1.15
hydroxylamine
-
25°C, pH 7.0, electron donor horse heart cytochrome c
1.38
hydroxylamine
-
25°C, pH 7.0, electron donor cytochrome c550
2.5
hydroxylamine
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor pseudoazurin
0.434
NH2OH

-
pre-reduced enzyme, electron donor horse heart cytochrome c
0.68
NH2OH
-
pre-reduced enzyme, electron donor cytochrome c550
1.15
NH2OH
-
initially oxidized enzyme, electron donor horse heart cytochrome c
1.38
NH2OH
-
initially oxidized enzyme, electron donor cytochrome c550
2.5
NH2OH
-
pre-reduced enzyme, electron donor pseudoazurin
0.00008
nitrite

-
25°C, A83D/A191E/G198E triple mutant
0.00024
nitrite
-
25°C, A191E/G198E double mutant
0.00025
nitrite
-
25°C, A83D/G198E double mutant
0.0003
nitrite
-
25°C, A83D/A191E double mutant
0.0005
nitrite
-
25°C, G198E mutant
0.00096
nitrite
-
25°C, A191E mutant
0.001
nitrite
-
25°C, A83D mutant
0.0013
nitrite
-
25°C, wild-type
0.006
nitrite
-
pH 6.2, 25°C, wild-type enzyme
0.007
nitrite
-
25°C, pH 7.0, electron donor cytochrome c550; 25°C, pH 7.0, electron donor horse heart cytochrome c
0.011
nitrite
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor horse heart cytochrome c
0.012
nitrite
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor cytochrome c550
0.019
nitrite
-
25°C, pH 7.0, electron donor pseudoazurin
0.034
nitrite
-
wild-type, pH 7.1
0.036
nitrite
-
25°C, pH 7.0
0.049
nitrite
-
25°C, pH 6.0
0.05
nitrite
-
mutant H254F, pH 7.1; mutant N90S, pH 7.1
0.053
nitrite
-
25°C, pH 6.5
0.063
nitrite
-
25°C, pH 7.0, Y25S mutant enzyme
0.068
nitrite
-
25°C, pH 7.5
0.071
nitrite
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor pseudoazurin
0.071
nitrite
-
25°C, pH 7.0, activated wild-type enzyme
0.099
nitrite
-
mutant enzyme M150H
0.22
nitrite
-
25°C, pH 8.0
0.25
nitrite
-
pH 6.5, 25°C
0.62
nitrite
-
25°C, pH 5.5
4.04
nitrite
pH and temperature not specified in the publication
9.5
nitrite
pH 7.4, temperature not specified in the publication
126
nitrite
-
mutant enzyme M150T
133
nitrite
-
mutant enzyme M150G
416
nitrite
-
wild-type enzyme
0.00147
NO2-

-
-
0.006
NO2-
-
recombinant wild-type enzyme
0.0073
NO2-
-
initially oxidized enzyme, electron donor horse heart cytochrome c
0.011
NO2-
-
pre-reduced enzyme, electron donor horse heart cytochrome c
0.012
NO2-
-
pre-reduced enzyme, electron donor cytochrome c550
0.0187
NO2-
-
initially oxidized enzyme, electron donor pseudoazurin
0.046
NO2-
-
reduced cytochrome c as electron donor
0.067
NO2-
-
initially oxidized enzyme, electron donor cytochrome c550
0.071
NO2-
-
pre-reduced enzyme, electron donor pseudoazurin
0.027
O2

-
cytochrome c oxidase activity
0.036
O2
-
wild-type enzyme
0.148
O2
-
pre-reduced enzyme, electron donor cytochrome c550
0.15
O2
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor cytochrome c550
0.16
O2
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor pseudoazurin
0.161
O2
-
pre-reduced enzyme, electron donor pseudoazurin
0.166
O2
-
pre-reduced enzyme, electron donor horse heart cytochrome c
0.17
O2
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor horse heart cytochrome c
0.21
O2
-
25°C, pH 7.0, electron donor cytochrome c550
0.214
O2
-
initially oxidized enzyme, electron donor cytochrome c550
0.47
O2
-
25°C, pH 7.0, electron donor horse heart cytochrome c; initially oxidized enzyme, electron donor horse heart cytochrome c
1
O2
-
mutant enzyme H369A
0.067
pseudoazurin

-
25°C, pH 6.0
-
0.077
pseudoazurin
-
25°C, pH 6.5
-
0.085
pseudoazurin
-
25°C, pH 8.0
-
0.1
pseudoazurin
-
25°C, pH 7.0
-
0.16
pseudoazurin
-
25°C, pH 7.5
-
additional information
additional information

-
-
-
additional information
additional information
-
steady-state kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7
Abz-VAA
-
25°C, pH 6.9, recombinant enzyme
1.33
cytochrome c
-
succinylated monomeric enzyme
0.583 - 2.8
cytochrome c551
-
796
ferricytochrome c551
pH 8.0, 25°C
-
0.025 - 0.043
Ferrocytochrome c-551
-
0.1
ferrocytochrome V(gamma)
-
-
-
additional information
additional information
-
-
-
1
azurin

-
recombinant Y10F mutant enzyme, at pH 6.2 and 27°C
1.12
azurin
-
recombinant wild-type enzyme, at pH 6.2 and 27°C
0.583
cytochrome c551

-
recombinant wild-type enzyme, at pH 6.2 and 27°C
-
0.6
cytochrome c551
-
recombinant Y10F mutant enzyme, at pH 6.2 and 27°C
-
2.8
cytochrome c551
-
at pH 7.0
-
0.025
Ferrocytochrome c-551

-
pH 6.2, 25°C, wild-type enzyme
-
0.032
Ferrocytochrome c-551
-
pH 6.2, 25°C, mutant enzyme H369A
-
0.043
Ferrocytochrome c-551
-
pH 6.2, 25°C, mutant enzyme H327A
-
0.08
hydroxylamine

-
25°C, pH 7.0, electron donor cytochrome c550
0.2
hydroxylamine
-
25°C, pH 7.0, electron donor horse heart cytochrome c
3
hydroxylamine
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor horse heart cytochrome c
3.2
hydroxylamine
-
25°C, pH 7.0, wild-type, pre-reduction with dithionite
3.5
hydroxylamine
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor cytochrome c550
6.4
hydroxylamine
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor pseudoazurin
7.7
hydroxylamine
-
25°C, pH 7.0, Y25S mutant enzyme
0.08
NH2OH

-
initially oxidized enzyme, electron donor cytochrome c550
0.2
NH2OH
-
initially oxidized enzyme, electron donor horse heart cytochrome c
3
NH2OH
-
pre-reduced enzyme, electron donor horse heart cytochrome c
3.5
NH2OH
-
pre-reduced enzyme, electron donor cytochrome c550
6.4
NH2OH
-
pre-reduced enzyme, electron donor pseudoazurin
0.08
nitrite

-
pH 6.2, 25°C, mutant enzyme H327A; pH 6.2, 25°C, mutant enzyme H369A
0.1
nitrite
pH 7.4, temperature not specified in the publication
0.62
nitrite
-
pH 7.0, electron donor azurin
2.1
nitrite
-
25°C, pH 7.0, electron donor cytochrome c550
2.4
nitrite
-
25°C, pH 7.0, electron donor horse heart cytochrome c
2.7
nitrite
-
25°C, pH 7.0, wild-type, without pre-reduction with dithionite
5.3
nitrite
-
25°C, pH 7.0, electron donor pseudoazurin
8
nitrite
-
pH 6.2, 25°C, wild-type enzyme
41
nitrite
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor horse heart cytochrome c
67
nitrite
-
25°C, pH 7.0, Y25S mutant enzyme
68
nitrite
-
25°C, pH 7.0, wild-type, pre-reduction with dithionite
71
nitrite
-
25°C, pH 8.0
74
nitrite
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor cytochrome c550
144
nitrite
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor pseudoazurin
219
nitrite
-
25°C, pH 7.5
243
nitrite
-
pH 7.0, electron donor benzyl viologen
320
nitrite
-
25°C, pH 5.5
392
nitrite
-
25°C, pH 7.0
1046
nitrite
-
25°C, pH 6.5
1478
nitrite
-
25°C, pH 6.0
38
NO

-
25°C, pH 6.5
0.08
NO2-

-
recombinant H327A and H369a mutant enzymes
2.1
NO2-
-
initially oxidized enzyme, electron donor cytochrome c550
2.4
NO2-
-
initially oxidized enzyme, electron donor horse heart cytochrome c
5.3
NO2-
-
initially oxidized enzyme, electron donor pseudoazurin
8
NO2-
-
recombinant wild-type enzyme
41
NO2-
-
pre-reduced enzyme, electron donor horse heart cytochrome c
74
NO2-
-
pre-reduced enzyme, electron donor cytochrome c550
80
NO2-
-
electron donor: reduced tetramethyl-4-phenylenediamine
106
NO2-
-
all-ferric nitrite-bound complex, electron donor pseudoazurin
144
NO2-
-
pre-reduced enzyme, electron donor pseudoazurin
0.11
O2

-
25°C, pH 7.0, electron donor horse heart cytochrome c; initially oxidized enzyme, electron donor horse heart cytochrome c
0.17
O2
-
25°C, pH 7.0, electron donor cytochrome c550; initially oxidized enzyme, electron donor cytochrome c550
2.8
O2
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor horse heart cytochrome c; pre-reduced enzyme, electron donor horse heart cytochrome c
3
O2
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor cytochrome c550; pre-reduced enzyme, electron donor cytochrome c550
3.2
O2
-
25°C, pH 7.0, wild-type, pre-reduction with dithionite
6.2
O2
-
25°C, pH 7.0, Y25S mutant enzyme
6.4
O2
-
25°C, pH 7.0, pre-reduced cytochrome cd1, electron donor pseudoazurin; pre-reduced enzyme, electron donor pseudoazurin
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