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Information on EC 1.7.2.6 - hydroxylamine dehydrogenase
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1.7.2.6 hydroxylamine dehydrogenaseIUBMB Comments
The enzymes from the nitrifying bacterium Nitrosomonas europaea [1,4] and the methylotrophic bacterium Methylococcus capsulatus are hemoproteins with seven c-type hemes and one specialized P-460-type heme per subunit. The enzyme converts hydroxylamine to nitrite via an enzyme-bound nitroxyl intermediate . While nitrite is the main product, the enzyme from Nitrosomonas europaea can also produce nitric oxide by catalysing the activity of EC 1.7.2.9, hydroxylamine oxidase .
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Word Map
- 1.7.2.6
- ammonia
- monooxygenase
-
nitrification
-
metagenomic
-
nitrify
- nitrospira
- europaea
- no2
- nitrosomonas
-
comammox
- phenylhydrazine
-
ammonium-oxidizing
-
genome-centric
- analysis
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
+
+
4
=
+
4
+
5
Synonyms
hydroxylamine dehydrogenase, nehao, nohao, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.7.3.4
-
-
formerly, part transferred
-
HAO
haoA
HCR
HOA
hydroxylamine oxidase
hydroxylamine oxidoreductase
hydroxylamine-cytochrome c reductase
hydroxylamine:oxygen oxidoreductase
mHAO
NeHAO
NirK
NoHAO
HAO
-
-
hydroxylamine oxidase
-
-
misleading
-
hydroxylamine oxidoreductase
-
-
ambiguous
-
hydroxylamine oxidoreductase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydroxylamine + H2O + 4 ferricytochrome c = nitrite + 4 ferrocytochrome c + 5 H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
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SYSTEMATIC NAME
IUBMB Comments
hydroxylamine:ferricytochrome-c oxidoreductase (nitrite-forming)
The enzymes from the nitrifying bacterium Nitrosomonas europaea [1,4] and the methylotrophic bacterium Methylococcus capsulatus [5] are hemoproteins with seven c-type hemes and one specialized P-460-type heme per subunit. The enzyme converts hydroxylamine to nitrite via an enzyme-bound nitroxyl intermediate [3]. While nitrite is the main product, the enzyme from Nitrosomonas europaea can also produce nitric oxide by catalysing the activity of EC 1.7.2.9, hydroxylamine oxidase [2].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
hydrazine + phenazine methosulfate
N2 + reduced phenazine methosulfate
-
-
-
?
hydroxylamine + 2,6-dichlorophenolindophenol
nitric oxide + oxidized 2,6-dichlorophenolindophenol + H+
-
-
-
-
?
hydroxylamine + 3 bovine ferricytochrome c
nitric oxide + 3 bovine ferrocytochrome c + 3 H+
hydroxylamine + 3 ferricytochrome c
nitric oxide + 3 ferrocytochrome c + 3 H+
-
-
-
?
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
nitrite + reduced 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide + H2O
NH3 + oxidized 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
hydroxylamine + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl-2H-tetrazolium bromide + H2O
nitrite + ?
hydroxylamine + cytochrome c
nitric oxide + oxidized cytochrome c + H+
-
-
-
-
?
hydroxylamine + ferricyanide
nitrite + ferrocyanide + H+
-
more than 90% of added hydroxylamine is oxidized to nitrite within 10 min when 10times as much ferricyanide as hydroxylamine is added
-
-
?
hydroxylamine + ferricyanide + H2O
nitric oxide + ferrocyanide + H+
-
high activity
-
-
?
hydroxylamine + ferricytochrome c554
nitric oxide + ferrocytochrome c554 + H+
-
-
-
-
?
hydroxylamine + H2O + 2,6-dichlorophenolindophenol
nitric oxide + reduced 2,6-dichlorophenolindophenol + H+
hydroxylamine + H2O + ferricytochrome c
nitrite + ferrocytochrome c + H+
-
-
-
-
r
hydroxylamine + H2O + horse heart cytochrome c
nitric oxide + reduced horse heart cytochrome c + H+
hydroxylamine + H2O + phenazine methosulfate
nitric oxide + reduced phenazine methosulfate + H+
hydroxylamine + N,N'-bis(carboxymethyl)-N,N'-dinitroso-1,4-phenylenediamine
nitric oxide + ?
-
-
-
-
?
hydroxylamine + phenazine methosulfate
nitric oxide + oxidized phenazine methosulfate + H+
-
-
-
-
?
hydroxylamine + reduced methyl viologen + H+
NH4+ + oxidized methyl viologen + H2O
-
-
-
-
ir
hydroxylamine + Ru(NH3)63+ + H+
nitric oxide + Ru(NH3)62+ + H+
-
-
-
-
ir
nitrite + reduced methyl viologen + H+
NH4+ + oxidized methyl viologen + H2O
-
HAO acts like a cytochrome c nitrite reductase, which catalyzes the six-electron reduction of nitrite to NH4+ by reduced methyl viologen
-
-
?
NO + H2O + ferricytochrome c
nitrite + ferrocytochrome c + 2 H+
-
-
-
-
r
hydroxylamine + 3 bovine ferricytochrome c
nitric oxide + 3 bovine ferrocytochrome c + 3 H+
-
-
-
-
?
hydroxylamine + 3 bovine ferricytochrome c
nitric oxide + 3 bovine ferrocytochrome c + 3 H+
-
-
-
-
?
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
nitrite + reduced 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
-
-
-
?
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
nitrite + reduced 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
-
-
-
?
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
nitrite + reduced 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
-
-
-
?
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
nitrite + reduced 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
-
-
-
?
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide + H2O
NH3 + oxidized 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
-
-
-
?
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide + H2O
NH3 + oxidized 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
-
-
-
?
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide + H2O
NH3 + oxidized 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
-
-
-
?
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide + H2O
NH3 + oxidized 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
-
-
-
?
hydroxylamine + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl-2H-tetrazolium bromide + H2O
nitrite + ?
-
-
-
-
?
hydroxylamine + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl-2H-tetrazolium bromide + H2O
nitrite + ?
-
-
-
-
?
hydroxylamine + ferricytochrome c + H2O
nitrite + ferrocytochrome c + H+
-
cytochrome c555 is able to accept electrons, but phenazine methosulfate is required for maximum enzyme activity
-
-
?
hydroxylamine + ferricytochrome c + H2O
nitrite + ferrocytochrome c + H+
-
-
-
-
?
hydroxylamine + ferricytochrome c + H2O
nitrite + ferrocytochrome c + H+
-
-
-
-
?
hydroxylamine + ferricytochrome c + H2O
nitrite + ferrocytochrome c + H+
-
-
394315, 394318, 394321, 394323, 394329, 394334, 639387, 656327, 657688, 657690, 657930, 658900, 658903, 696882, 710728, 719635
-
-
?
hydroxylamine + ferricytochrome c + H2O
nitrite + ferrocytochrome c + H+
-
-
-
-
ir
hydroxylamine + ferricytochrome c + H2O
nitrite + ferrocytochrome c + H+
-
in presence of diethyldithiocarbamate, hydroxylamine is oxidized to nitrite, for each mol of nitrite produced approximately 1 mol of diethyldithiocarbamate is oxidized to bis(diethyldithiocarbamoyl)disulfide
-
?
hydroxylamine + ferricytochrome c + H2O
nitrite + ferrocytochrome c + H+
-
Nitrosomonas cytochrome c-554 can act as electron carrier
-
?
hydroxylamine + ferricytochrome c + H2O
nitrite + ferrocytochrome c + H+
-
mammalian cytochrome c can serve as electron acceptor
-
-
?
hydroxylamine + ferricytochrome c + H2O
nitrite + ferrocytochrome c + H+
-
energy production
-
?
hydroxylamine + ferricytochrome c + H2O
nitrite + ferrocytochrome c + H+
-
-
-
-
?
hydroxylamine + ferricytochrome c + H2O
nitrite + ferrocytochrome c + H+
-
-
-
-
?
hydroxylamine + ferricytochrome c + H2O
nitrite + ferrocytochrome c + H+
-
-
-
-
?
hydroxylamine + ferricytochrome c + H2O
nitrite + ferrocytochrome c + H+
-
-
-
-
?
hydroxylamine + ferricytochrome c-554 + H2O
nitrite + ferrocytochrome c-554 + H+
-
-
-
?
hydroxylamine + ferricytochrome c-554 + H2O
nitrite + ferrocytochrome c-554 + H+
-
-
-
?
hydroxylamine + ferricytochrome c554 + H2O
nitrite + ferrocytochrome c554 + H+
-
-
-
-
?
hydroxylamine + ferricytochrome c554 + H2O
nitrite + ferrocytochrome c554 + H+
-
-
-
?
hydroxylamine + ferricytochrome c554 + H2O
nitrite + ferrocytochrome c554 + H+
-
ferricytochrome is a c554 better electron acceptor than horse heart cytochrome c
-
-
?
hydroxylamine + ferricytochrome c554 + H2O
nitrite + ferrocytochrome c554 + H+
-
-
-
-
?
hydroxylamine + ferricytochrome c554 + H2O
nitrite + ferrocytochrome c554 + H+
-
-
-
-
?
hydroxylamine + H2O + 2 ferricyanide
nitrite + 2 ferrocyanide + 5 H+
-
-
-
?
hydroxylamine + H2O + 2 ferricyanide
nitrite + 2 ferrocyanide + 5 H+
-
-
-
?
hydroxylamine + H2O + 2,6-dichlorophenolindophenol
nitric oxide + reduced 2,6-dichlorophenolindophenol + H+
-
very low activity
-
-
?
hydroxylamine + H2O + 2,6-dichlorophenolindophenol
nitric oxide + reduced 2,6-dichlorophenolindophenol + H+
-
very low activity
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
-
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
-
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
-
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
via NO as intermediate
-
-
r
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
via NO as intermediate
-
-
r
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
-
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
-
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
usage of horse heart cytochrome c
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
-
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
usage of horse heart cytochrome c
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
usage of horse heart cytochrome c
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
usage of horse heart cytochrome c
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
-
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
usage of horse heart cytochrome c
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
-
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
usage of horse heart cytochrome c
-
-
?
hydroxylamine + H2O + benzylviologen
NO + reduced benzylviologen + 2 H+
-
-
-
-
?
hydroxylamine + H2O + benzylviologen
NO + reduced benzylviologen + 2 H+
-
-
-
-
?
hydroxylamine + H2O + ferricyanide
nitric oxide + ferrocyanide + H+
-
best electron acceptor
-
-
?
hydroxylamine + H2O + ferricyanide
nitric oxide + ferrocyanide + H+
-
best electron acceptor
-
-
?
hydroxylamine + H2O + horse heart cytochrome c
nitric oxide + reduced horse heart cytochrome c + H+
-
very low activity
-
-
?
hydroxylamine + H2O + horse heart cytochrome c
nitric oxide + reduced horse heart cytochrome c + H+
-
very low activity
-
-
?
hydroxylamine + H2O + methylviologen
NO + reduced methylviologen + 2 H+
-
-
-
-
?
hydroxylamine + H2O + methylviologen
NO + reduced methylviologen + 2 H+
-
-
-
-
?
hydroxylamine + H2O + NAD+
nitric oxide + NADH + H+
-
very low activity
-
-
?
hydroxylamine + H2O + NAD+
nitric oxide + NADH + H+
-
very low activity
-
-
?
hydroxylamine + H2O + phenazine methosulfate
nitric oxide + reduced phenazine methosulfate + H+
-
very low activity, in the presence of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
-
?
hydroxylamine + H2O + phenazine methosulfate
nitric oxide + reduced phenazine methosulfate + H+
-
very low activity, in the presence of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
-
?
hydroxylamine + O2
nitrite + H2O
-
phenazine methosulfate, dichlorophenolindophenol, mammalian cytochrome c and 3-(4,5-dimethylthiazolyl-2)-2,5-diphenyltetrazolium chloride can serve as electron acceptors
-
?
hydroxylamine + phenazine methosulfate + H2O
NH3 + oxidized phenazine methosulfate
-
-
-
-
?
hydroxylamine + phenazine methosulfate + H2O
NH3 + oxidized phenazine methosulfate
-
-
-
-
?
hydroxylamine + phenazine methosulfate + H2O
NH3 + oxidized phenazine methosulfate
-
-
-
-
?
hydroxylamine + phenazine methosulfate + H2O
NH3 + oxidized phenazine methosulfate
-
-
-
-
?
hydroxylamine + phenazine methosulfate + H2O
nitrite + ?
-
-
-
-
?
nitrite + reduced benzyl viologen + H+
NH4+ + reduced methyl viologen + H2O
-
-
-
-
?
nitrite + reduced benzyl viologen + H+
NH4+ + reduced methyl viologen + H2O
-
-
-
-
?
nitrite + reduced benzyl viologen + H+
NH4+ + reduced methyl viologen + H2O
-
-
-
-
?
nitrite + reduced benzyl viologen + H+
NH4+ + reduced methyl viologen + H2O
-
-
-
-
?
NO + ferrocytochrome c + 2 H+
hydroxylamine + H2O + ferricytochrome c
-
-
-
-
r
NO + ferrocytochrome c + 2 H+
hydroxylamine + H2O + ferricytochrome c
-
-
-
-
r
additional information
?
-
-
hydroxylamine oxidation is negligible
-
-
?
additional information
?
-
-
hydroxylamine oxidation is negligible
-
-
?
additional information
?
-
-
enzyme HAO can catalyze the interconversion of NO and NH2OH. The enzyme catalyzes a three-electron oxidation of NH2OH to NO using bovine cytochrome c as an oxidant. Strain KSU-1 catalyzes the reduction of NO with reduced benzyl viologen (BVred) and the NO-releasing reagent hydroxy-2-oxo-3-(N-methyl-3-amino-propyl)-3-methyl-1-triazene, i.e. NOC 7. Substrate specificity of strain KSU-1 enzyme HAO, overview
-
-
?
additional information
?
-
-
enzyme HAO can catalyze the interconversion of NO and NH2OH. The enzyme catalyzes a three-electron oxidation of NH2OH to NO using bovine cytochrome c as an oxidant. Strain KSU-1 catalyzes the reduction of NO with reduced benzyl viologen (BVred) and the NO-releasing reagent hydroxy-2-oxo-3-(N-methyl-3-amino-propyl)-3-methyl-1-triazene, i.e. NOC 7. Substrate specificity of strain KSU-1 enzyme HAO, overview
-
-
?
additional information
?
-
-
hydroxylamine oxidation is negligible
-
-
?
additional information
?
-
-
optimization of HAO activity assay method, evaluation, overview
-
-
?
additional information
?
-
-
optimization of HAO activity assay method, evaluation, overview
-
-
?
additional information
?
-
-
HAO does not catalyze the disproportionation of hydroxylamine, despite the thermodynamic favorability of such a process, and the apparent opportunity presented by the HAO structure
-
-
?
additional information
?
-
-
oxidation of hydroxylamine by the enzyme results in the production of a mixture of HNO2/HNO3
-
-
?
additional information
?
-
optimization of HAO activity assay method, evaluation, overview
-
-
?
additional information
?
-
-
optimization of HAO activity assay method, evaluation, overview
-
-
?
additional information
?
-
optimization of HAO activity assay method, evaluation, overview
-
-
?
additional information
?
-
-
oxidation of hydroxylamine by the enzyme results in the production of a mixture of HNO2/HNO3
-
-
?
additional information
?
-
-
optimization of HAO activity assay method, evaluation, overview
-
-
?
additional information
?
-
enzyme catalyzes the reduction of NO2- to NO, the oxidation of hydroxylamine (NH2OH) to NO, reaction of EC 1.7.2.6, and the production of N2O from NH2OH and NO2
-
-
-
additional information
?
-
enzyme catalyzes the reduction of NO2- to NO, the oxidation of hydroxylamine (NH2OH) to NO, reaction of EC 1.7.2.6, and the production of N2O from NH2OH and NO2
-
-
-
additional information
?
-
-
optimization of HAO activity assay method, evaluation, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
hydroxylamine + ferricytochrome c + H2O
nitrite + ferrocytochrome c + H+
-
-
-
-
?
hydroxylamine + ferricytochrome c + H2O
nitrite + ferrocytochrome c + H+
-
-
-
-
ir
hydroxylamine + ferricytochrome c + H2O
nitrite + ferrocytochrome c + H+
-
energy production
-
?
hydroxylamine + ferricytochrome c + H2O
nitrite + ferrocytochrome c + H+
-
-
-
-
?
hydroxylamine + ferricytochrome c554 + H2O
nitrite + ferrocytochrome c554 + H+
-
-
-
-
?
hydroxylamine + ferricytochrome c554 + H2O
nitrite + ferrocytochrome c554 + H+
-
-
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
-
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
-
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
-
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
via NO as intermediate
-
-
r
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
via NO as intermediate
-
-
r
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
-
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
-
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
-
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
-
-
-
?
hydroxylamine + H2O + 4 ferricytochrome c
nitrite + 4 ferrocytochrome c + 5 H+
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochrome c
purified enzyme shows typical cytochrome-like absorption spectra, but with a peculiar peak at 468 nm in the reduced state that is due to a P460 moiety corresponding to a modified heme c molecule
heme
-
-
heme
-
each alpha,beta subunit of the (alpha,beta)3 subunit structure contains 7-8 c-type hemes and one prosthetic group P-460, P-460 is a MW 17000 protein fragment
heme
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resolution of the hemes by redox potentiometry and electron spin resonance spectroscopy
heme
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enzyme consists of one alpha-beta-3 subunit and contains seven-eight c-type hemes and P460
heme