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Information on EC 1.7.2.8 - hydrazine dehydrogenase
for references in articles please use BRENDA:EC1.7.2.8
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EC Tree 1 Oxidoreductases
1.7 Acting on other nitrogenous compounds as donors
1.7.2 With a cytochrome as acceptor
1.7.2.8 hydrazine dehydrogenase
IUBMB Comments
The enzyme, which is involved in the pathway of anaerobic ammonium oxidation in anammox bacteria, has been purified from the bacterium Candidatus Kuenenia stuttgartiensis. The electrons derived from hydrazine are eventually transferred to the quinone pool.
The enzyme appears in viruses and cellular organisms
- 1.7.2.8
-
anammox
- nitrite
- rrna
-
candidatus
-
ammonium-oxidizing
- kuenenia
- scalindua
-
wastewater
-
reactor
- brocadia
- stuttgartiensis
- sludge
- anammoxosome
-
planctomycete
- nitrosomonas
-
oxygen-limited
-
biogeochemical
-
influent
-
ladderane
-
wetland
-
denitrification
- jettenia
-
dinitrogen
-
denitrifiers
- environmental protection
Reaction Schemes
showSynonyms
hydrazine dehydrogenase, hydrazine oxidoreductase, hydrazine-oxidizing enzyme, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.7.99.8
-
-
formerly
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HAO
HDH
hydrazine oxidoreductase
-
-
-
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hydroxylamine oxidoreductase
HAO
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-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrazine + 4 ferricytochrome c = N2 + 4 ferrocytochrome c
-
-
-
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hydroxylamine + NH3 + acceptor = N2 + H2O + reduced acceptor
catalytic mechanism, overview
-
hydroxylamine + NH3 + acceptor = N2 + H2O + reduced acceptor
the meso tyrosyl residue enhances the binding of hydroxylamine, and increases the stability of a FeIIINO intermediate, while behaving indifferently in the FeIINO form, catalytic mechanism, modelling, overview
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hydroxylamine + NH3 + acceptor = N2 + H2O + reduced acceptor
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
ammonia oxidation II (anaerobic)
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SYSTEMATIC NAME
IUBMB Comments
hydrazine:ferricytochrome c oxidoreductase
The enzyme, which is involved in the pathway of anaerobic ammonium oxidation in anammox bacteria, has been purified from the bacterium Candidatus Kuenenia stuttgartiensis. The electrons derived from hydrazine are eventually transferred to the quinone pool.
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CAS REGISTRY NUMBER
COMMENTARY
9075-43-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
hydrazine + 2,6-dichloroindophenol
? + reduced 2,6-dichloroindophenol
Substrates: -
Products: -
Products: -
?
hydrazine + 2,6-dichlorophenolindophenol
N2 + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
hydrazine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
? + reduced methylthiazolyltetrazolium bromide
Substrates: reduction of 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide via phenazine methosulfate
Products: -
Products: -
?
hydrazine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
N2 + reduced 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
Substrates: -
Products: -
Products: -
?
hydrazine + 4 bovine heart ferricytochrome c
N2 + 4 bovine heart ferrocytochrome c
-
Substrates: -
Products: -
Products: -
?
hydrazine + ferricyanide
? + ferrocyanide
Substrates: -
Products: -
Products: -
?
hydrazine + ferricyanide
N2 + ferrocyanide
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Substrates: ferricyanide as the electron acceptor results in the highest specific activity. Hydrazine is solely converted to N2
Products: -
Products: -
?
hydrazine + ferricytochrome
N2 + ferrocytochrome
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Substrates: horse heart cytochrome. Hydrazine is solely converted to N2
Products: -
Products: -
?
hydrazine + ferricytochrome c
? + ferrocytochrome c
Substrates: -
Products: -
Products: -
?
hydrazine + methylthiazolyltetrazolium bromide
? + reduced methylthiazolyltetrazolium bromide
Substrates: reduction of methylthiazolyltetrazolium bromide via phenazine methosulfate
Products: -
Products: -
?
hydrazine + methylthiazolyltetrazolium bromide
N2 + reduced methylthiazolyltetrazolium bromide
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Substrates: reduction of methylthiazolyltetrazolium bromide via phenazine methosulfate. Hydrazine is solely converted to N2
Products: -
Products: -
?
hydrazine + NH3 + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
?
Substrates: -
Products: -
Products: -
?
hydrazine + NH3 + phenazine methosulfate
?
Substrates: -
Products: -
Products: -
?
hydrazine + phenazine methosulfate
? + reduced phenazine methosulfate
Substrates: -
Products: -
Products: -
?
hydroxylamine + 2 acceptor + H2O
nitrite + 2 reduced acceptor + H+
-
Substrates: -
Products: -
Products: -
?
hydroxylamine + 2,6-dichlorophenolindophenol
N2O + reduced 2,6-dichlorophenolindophenol
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Substrates: horse heart cytochrome. The conversion of hydroxylamine by the enzyme results in the formation of NO and N2O. A small amount of NO2- is measured, but this is probably due to the chemical reaction of NO. No other nitrogen compounds are detected
Products: small amounts of NO are also formed
Products: small amounts of NO are also formed
?
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
? + reduced 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
Substrates: reduction of methylthiazolyltetrazolium bromide via phenazine methosulfate
Products: -
Products: -
?
hydroxylamine + ferricyanide
N2O + ferrocyanide
-
Substrates: ferricyanide as the electron acceptor results in the highest specific activity. The conversion of hydroxylamine by the enzyme results in the formation of NO and N2O. A small amount of NO2- is measured, but this is probably due to the chemical reaction of NO. No other nitrogen compounds are detected
Products: small amounts of NO are also formed
Products: small amounts of NO are also formed
?
hydroxylamine + ferricytochrome
N2O + ferrocytochrome
-
Substrates: horse heart cytochrome. The conversion of hydroxylamine by the enzyme results in the formation of NO and N2O. A small amount of NO2- is measured, but this is probably due to the chemical reaction of NO. No other nitrogen compounds are detected
Products: small amounts of NO are also formed
Products: small amounts of NO are also formed
?
hydroxylamine + methylthiazolyltetrazolium bromide
N2O + reduced methylthiazolyltetrazolium bromide
-
Substrates: the conversion of hydroxylamine by the enzyme results in the formation of NO and N2O. A small amount of NO2- is measured, but this is probably due to the chemical reaction of NO. No other nitrogen compounds are detected
Products: small amounts of NO are also formed
Products: small amounts of NO are also formed
?
hydroxylamine + NH3 + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
?
Substrates: -
Products: -
Products: -
?
hydroxylamine + NH3 + phenazine methosulfate
NO2 + H2O + reduced phenazine methosulfate
Substrates: -
Products: -
Products: -
?
hydrazine + 4 ferricytochrome c
N2 + 4 ferrocytochrome c
-
Substrates: -
Products: -
Products: -
?
hydrazine + 4 ferricytochrome c
N2 + 4 ferrocytochrome c
-
Substrates: -
Products: -
Products: -
?
hydrazine + 4 ferricytochrome c
N2 + 4 ferrocytochrome c
-
Substrates: -
Products: -
Products: -
?
hydrazine + ferricytochrome c
N2 + ferrocytochrome c
-
Substrates: -
Products: -
Products: -
?
hydrazine + ferricytochrome c
N2 + ferrocytochrome c
-
Substrates: -
Products: -
Products: -
?
hydrazine + ferricytochrome c
N2 + ferrocytochrome c
-
Substrates: highly specific for hydrazine oxidation activity
Products: -
Products: -
?
hydroxylamine + NH3 + cytochrome c-554
NO2 + H2O + reduced cytochrome c-554
-
Substrates: -
Products: -
Products: -
?
hydroxylamine + NH3 + cytochrome c-554
NO2 + H2O + reduced cytochrome c-554
-
Substrates: the ammonia-oxidizing bacterium Nitrosomonas europaea normally catalyzes the four-electron oxidation of hydroxylamine to nitrite, which is the second step in ammonia-dependent respiration. In the presence of methyl viologen monocation radical, HAO can catalyze the reduction of nitric oxide to ammonia, reaction of by cytochrome c nitrite reductase , EC 1.7.2.2, overview
Products: -
Products: -
?
additional information
?
-
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Substrates: the enzyme is involved in anaerobic ammonium oxidation. Anaerobic ammonium oxidation is very important in the oceanic nitrogen cycle
Products: -
Products: -
?
additional information
?
-
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Substrates: the enzyme is involved in the anaerobic oxidation of ammonium
Products: -
Products: -
?
additional information
?
-
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Substrates: the enzyme is involved in the pathway of anaerobic ammonium oxidation
Products: -
Products: -
?
additional information
?
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Substrates: methanol is not a substrate, no activity with NAD+, benzyl viologen and Wurster's blue. The enzyme from anaerobic ammonium-oxidizing (Anammox) enrichment culture is also capable of reducing NO to N2O with a specific activity of 2.9 units/mg at room temperature. Reduction of nitrite in the presence of reduced methyl viologen results in the production of N2O and some NO (below 5%). No other nitrogen compounds are detected. In the presence of ascorbate and PMS, no nitrite conversion is observed
Products: -
Products: -
?
additional information
?
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Substrates: HAO is an indispensable enzyme and well conserved in anammox bacteria
Products: -
Products: -
?
additional information
?
-
Substrates: HAO is an indispensable enzyme and well conserved in anammox bacteria
Products: -
Products: -
?
additional information
?
-
Substrates: hydrazine-oxidizing enzyme (HZO, wich has no activity with hydroxylamine) and hydroxylamine oxidoreductase (HAO, which oxidizes hydroxylamine and hydrazine) occur both in planctomycete KSU-1
Products: -
Products: -
?
additional information
?
-
-
Substrates: hydrazine-oxidizing enzyme (HZO, wich has no activity with hydroxylamine) and hydroxylamine oxidoreductase (HAO, which oxidizes hydroxylamine and hydrazine) occur both in planctomycete KSU-1
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with NAD+, hydroxylamine is not a substrate for hydrazine-oxidizing enzyme HZOB
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with NAD+, hydroxylamine is not a substrate for hydrazine-oxidizing enzyme HZOB
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in anaerobic ammonium oxidation. Anaerobic ammonium oxidation is very important in the oceanic nitrogen cycle
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the anaerobic oxidation of ammonium
Products: -
Products: -
?
additional information
?
-
-
Substrates: hydroxylamine does not serve as a substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme shows hydroxylamine oxidase, hydrazine oxidase, and nitrite reductase activities
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in anaerobic ammonium oxidation. Anaerobic ammonium oxidation is very important in the oceanic nitrogen cycle
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the conversion of hydroxylamine to nitrite, with a complicate arrangement of heme groups in three subunits
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the four-electron oxidation of NH2OH to nitrite under aerobic conditions, HAO reacts with NO radical and NH2OH under reducing conditions
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
hydroxylamine + 2 acceptor + H2O
nitrite + 2 reduced acceptor + H+
-
Substrates: -
Products: -
Products: -
?
hydroxylamine + NH3 + cytochrome c-554
NO2 + H2O + reduced cytochrome c-554
-
Substrates: the ammonia-oxidizing bacterium Nitrosomonas europaea normally catalyzes the four-electron oxidation of hydroxylamine to nitrite, which is the second step in ammonia-dependent respiration. In the presence of methyl viologen monocation radical, HAO can catalyze the reduction of nitric oxide to ammonia, reaction of by cytochrome c nitrite reductase , EC 1.7.2.2, overview
Products: -
Products: -
?
hydrazine + 4 ferricytochrome c
N2 + 4 ferrocytochrome c
-
Substrates: -
Products: -
Products: -
?
hydrazine + 4 ferricytochrome c
N2 + 4 ferrocytochrome c
-
Substrates: -
Products: -
Products: -
?
hydrazine + 4 ferricytochrome c
N2 + 4 ferrocytochrome c
-
Substrates: -
Products: -
Products: -
?
hydrazine + ferricytochrome c
N2 + ferrocytochrome c
-
Substrates: -
Products: -
Products: -
?
hydrazine + ferricytochrome c
N2 + ferrocytochrome c
-
Substrates: -
Products: -
Products: -
?
hydrazine + ferricytochrome c
N2 + ferrocytochrome c
-
Substrates: highly specific for hydrazine oxidation activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in anaerobic ammonium oxidation. Anaerobic ammonium oxidation is very important in the oceanic nitrogen cycle
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the anaerobic oxidation of ammonium
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the pathway of anaerobic ammonium oxidation
Products: -
Products: -
?
additional information
?
-
-
Substrates: HAO is an indispensable enzyme and well conserved in anammox bacteria
Products: -
Products: -
?
additional information
?
-
Substrates: HAO is an indispensable enzyme and well conserved in anammox bacteria
Products: -
Products: -
?
additional information
?
-
Substrates: hydrazine-oxidizing enzyme (HZO, wich has no activity with hydroxylamine) and hydroxylamine oxidoreductase (HAO, which oxidizes hydroxylamine and hydrazine) occur both in planctomycete KSU-1
Products: -
Products: -
?
additional information
?
-
-
Substrates: hydrazine-oxidizing enzyme (HZO, wich has no activity with hydroxylamine) and hydroxylamine oxidoreductase (HAO, which oxidizes hydroxylamine and hydrazine) occur both in planctomycete KSU-1
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in anaerobic ammonium oxidation. Anaerobic ammonium oxidation is very important in the oceanic nitrogen cycle
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the anaerobic oxidation of ammonium
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in anaerobic ammonium oxidation. Anaerobic ammonium oxidation is very important in the oceanic nitrogen cycle
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
coenzyme Q
-
CoQ, an essential component participating in the electron transfer from enzyme HDH to cytochrome bc1 complex. HDH activity can be recovered with exogenous CoQ addition
cytochrome c554
-
a soluble 26.1-kDa tetraheme protein that is quite abundant in the periplasm of Nitrosomas europaea and is the acceptor of the electrons from HAO in vivo
cytochrome P460
-
cytochrome P460 heme, c-type heme, and planar heme, structure modelling, overview
-
cytochrome P468
the enzyme has a cytochrome P468 chromophore
-
heme
the hao gene indicats eight c-type heme binding motifs and is a multiheme protein containing covalently bound c-type heme
additional information
-
the sequence deduced from the hao gene indicates eight c-type heme binding motifs
-
additional information
the sequence deduced from the hao gene indicates eight c-type heme binding motifs
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cyanide
-
addition of 0.035 mM, 0.085 mM, or 0.35 mM cyanide results in 25%, 50%, and 95% inhibition, respectively
H2O2
-
0.0004 mM, 0.004 mM, and 0.04 mM results in a loss of activity of 30%, 75%, and 90%, respectively
hydrazine
-
competes strongly with hydroxylamine. Addition of 0.015 mM, 0.035 mM, and 0.35 mM results in 15%, 50%, and 85% inhibition, respectively
SDS
-
activity in the presence of 0.75%, 3%, and 8% SDS is reduced by 20%, 50%, and 95%, respectively
additional information
-
sodium azide, methanol, sodium nitrite, and the chelating agent EDTA do not inhibit enzyme activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
reduced graphene oxide
-
RGO, highly activating, optimal at 100 mg/l in the nedium
-
additional information
-
reduced graphene oxide has much better electron transfer ability compared to coenzyme Q, resulting in a higher activation of the enzyme
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics, both reaction steps show first-order dependence on nitric oxide
-
0.018
hydrazine
-
pH 8.0, 35°C, reduction of methylthiazolyltetrazolium bromide via phenazine methosulfate
0.026
hydroxylamine
-
pH 8.0, 35°C, reduction of methylthiazolyltetrazolium bromide via phenazine methosulfate
0.127
hydroxylamine
-
pH 8.0, 65°C, reduction of methylthiazolyltetrazolium bromide via phenazine methosulfate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.6
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
65
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
hydroxylamine oxidoreductase is purified and characterized from an anaerobic ammonium-oxidizing (Anammox) enrichment culture
-
-
brenda