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Information on EC 1.12.2.1 - cytochrome-c3 hydrogenase
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1.12.2.1 cytochrome-c3 hydrogenaseIUBMB Comments
An iron-sulfur protein. Some forms of the enzyme contain nickel ([NiFe]-hydrogenases) and, of these, some contain selenocysteine ([NiFeSe]-hydrogenases). Methylene blue and other acceptors can also be reduced.
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Word Map
- 1.12.2.1
- hydrogenases
- desulfovibrio
- nickel
-
hydride
- eutropha
-
h-cluster
-
iron-sulfur
- ralstonia
-
o2-tolerant
- nife-hydrogenases
- hildenborough
-
dihydrogen
-
hyperfine
-
electrochemistry
-
diiron
-
sulfate-reducing
- fe-hydrogenase
- miyazaki
-
heterolytic
- desulfuricans
-
oxygen-tolerant
-
electrocatalytic
-
allochromatium
-
metallochaperone
-
overpotential
-
subcluster
- pasteurianum
- fructosovorans
-
organometallic
- hydf
-
dinuclear
-
bimetallic
-
co-inhibited
-
nickel-iron
- vinosum
-
h2-oxidizing
-
hydrogen-producing
-
maturase
- environmental protection
- fhl
-
tetraheme
- industry
-
metallocenter
- hydrogenlyase
-
hyscore
-
nickel-binding
- synthesis
-
h2-dependent
-
electrocatalysts
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
[nife] hydrogenase, [nife]-hydrogenase, [fefe] hydrogenase, [fe]-hydrogenase, [fe] hydrogenase, h2ase, fe-only hydrogenase, [nifese] hydrogenase, hydab, [nifese] hase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cytochrome c3 hydrogenase
-
-
-
-
cytochrome c3 reductase
-
-
-
-
cytochrome hydrogenase
-
-
-
-
cytochrome-c3 hydrogenase
Fe-only hydrogenase
H2:ferricytochrome c3 oxidoreductase
-
-
-
-
H2ase
hyd B
HydAB
hydrogenase
-
-
-
-
hydrogenase, cytochrome
-
-
-
-
HysAB
[FeFe] hydrogenase
[Fe] hydrogenase
[NiFeSe] Hase
[NiFeSe] hydrogenase
[NiFe] Hase
[NiFe] hydrogenase
[NiFe]-hydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
H2 + 2 ferricytochrome c3 = 2 H+ + 2 ferrocytochrome c3
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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-
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SYSTEMATIC NAME
IUBMB Comments
hydrogen:ferricytochrome-c3 oxidoreductase
An iron-sulfur protein. Some forms of the enzyme contain nickel ([NiFe]-hydrogenases) and, of these, some contain selenocysteine ([NiFeSe]-hydrogenases). Methylene blue and other acceptors can also be reduced.
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CAS REGISTRY NUMBER
COMMENTARY
9027-05-8
-
9079-91-8
-
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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
Fe(III)-nitrilotriacetate + ferricytochrome c3
Fe(II)-nitrilotriacetate + ferrocytochrome c3
ferricytochrome c3 + 2 H2
ferrocytochrome c3 + 4 H+
-
48% relative activity compared to activity with oxidized methyl viologen
-
-
?
H2 + acceptor
H+ + reduced acceptor
electrode-grown cells overexpress the hyn-1 gene for [NiFe] hydrogenase 1
-
-
?
H2 + ferredoxin
H+ + reduced ferredoxin
Megalodesulfovibrio gigas
-
requires the presence of cytochrome c3 for the reduction of ferredoxin
-
-
?
H2 + oxidized dichloroindophenol
H+ + ?
-
30% relative activity compared to activity with oxidized methyl viologen
-
-
?
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
100% relative activity
-
-
?
H2 + potassium ferricyanide
H+ + ?
-
34% relative activity compared to activity with oxidized methyl viologen
-
-
?
H2 + rubredoxin
H+ + reduced rubredoxin
Megalodesulfovibrio gigas
-
requires the presence of cytochrome c3 for the reduction of rubredoxin
-
-
?
lactate + ferrocytochrome c3
pyruvate + ferricytochrome c3
-
-
-
-
?
pyruvate + ferrocytochrome c3
lactate + ferricytochrome c3
-
-
-
-
?
Fe(III)-nitrilotriacetate + ferricytochrome c3
Fe(II)-nitrilotriacetate + ferrocytochrome c3
-
-
-
-
?
Fe(III)-nitrilotriacetate + ferricytochrome c3
Fe(II)-nitrilotriacetate + ferrocytochrome c3
-
-
-
-
?
H+ + ferrocytochrome c3
H2 + ferricytochrome c3
-
-
-
-
?
H+ + reduced methyl viologen
H2 + methyl viologen
-
weak activity in H2-uptake assay
-
-
r
H+ + reduced methyl viologen
H2 + methyl viologen
-
-
-
-
?
H2 + ammonium pertechnetate
?
-
the reaction requires the presence of c-type cytochromes
-
-
?
H2 + ammonium pertechnetate
?
Shewanella oneidensis MR-1 / ATCC 700550
-
the reaction requires the presence of c-type cytochromes
-
-
?
H2 + benzyl viologen
H+ + reduced benzyl viologen
-
-
-
r
H2 + ferricytochrome c
H+ + ferrocytochrome c
-
nonaheme cytochrome c
-
-
?
H2 + ferricytochrome c
H+ + ferrocytochrome c
-
nonaheme cytochrome c
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
the type I cytochrome C3 complex is more efficient than type II cytochrome c3 complex as electron acceptor from hydrogenase
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
isoform type I cytochrome c3 has the potential to transfer two electrons at a time. The two isoforms type I and type II cytochrome c3 are physiological partners but only single-electron transfers occur in solution
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-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
-
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
-
-
-
r
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
tetraheme cytochrome c3
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-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
cytochrome c3 receives two protons and two electrons from hydrogenase for transport to the membrane, and converting electronic energy into proton motive force
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
tetraheme cytochrome c3
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
-
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
-
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
part of an electron transport chain that mediates electronic coupling between periplasmic hydrogen oxidation and cytosolic sulfate reduction
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r
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
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13 kDa tetraheme cytochrome c3 forms a complex with a hexadecaheme high molecular weight cytochrome c, i.e. Hmc
-
-
r
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
the positive charges of Lys60, Lys72, Lys95, and Lys101 around heme 4 are important for formation of the transient complex with [NiFe] hydrogenase in the initial stage of the cytochrome c3 reduction. Reaction with wild-type and mutant cytochrome c3
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
-
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
part of an electron transport chain that mediates electronic coupling between periplasmic hydrogen oxidation and cytosolic sulfate reduction
-
-
r
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
13 kDa tetraheme cytochrome c3 forms a complex with a hexadecaheme high molecular weight cytochrome c, i.e. Hmc
-
-
r
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
-
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
-
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
the positive charges of Lys60, Lys72, Lys95, and Lys101 around heme 4 are important for formation of the transient complex with [NiFe] hydrogenase in the initial stage of the cytochrome c3 reduction. Reaction with wild-type and mutant cytochrome c3
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
Megalodesulfovibrio gigas
-
-
-
-
?
H2 + ferricytochrome Hmc
H+ + ferrocytochrome Hmc
-
13 kDa tetraheme cytochrome c3 forms a complex with a hexadecaheme high molecular weight cytochrome c, i.e. Hmc
-
-
r
H2 + ferricytochrome Hmc
H+ + ferrocytochrome Hmc
-
13 kDa tetraheme cytochrome c3 forms a complex with a hexadecaheme high molecular weight cytochrome c, i.e. Hmc
-
-
r
H2 + methylene blue
H+ + reduced methylene blue
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the reation is dependent on the presence of b-type cytochrome HupZ
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-
r
H2 + methylene blue
H+ + reduced methylene blue
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the reation is dependent on the presence of b-type cytochrome HupZ
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-
r
H2 + methylene blue
H+ + reduced methylene blue
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no activity in H2-evolution assay
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-
ir
H2 + methylene blue
H+ + reduced methylene blue
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no activity in H2-evolution assay
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-
ir
H2 + methylviologen-dication
H+ + methylviologen
-
-
-
?
H2 +[Fe] hydrogenase-cytochrome c3-cytochrome Hmc complex
?
-
-
-
-
r
lactate + ammonium pertechnetate
?
-
the reaction requires the presence of c-type cytochromes
-
-
?
lactate + ammonium pertechnetate
?
Shewanella oneidensis MR-1 / ATCC 700550
-
the reaction requires the presence of c-type cytochromes
-
-
?
reduced methyl viologen + H+
oxidized methyl viologen + H2
-
-
-
-
?
additional information
?
-
-
hydrogen-dependent platinum (IV) reducing activity in the presence of hydrogenase and its physiological electron carrier, cytochrome c3
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-
?
additional information
?
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-
cytochrome c3 is the natural electron acceptor
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-
?
additional information
?
-
-
enzyme catalyzes production of H2 from Na2S2O4 in presence of cytochrome c3
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-
?
additional information
?
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-
enzyme can catalyze H-2H exchange in absence of added electron carriers
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-
?
additional information
?
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-
no reduction of ferredoxin, methylene blue or hexacyanoferrate(II) by H2
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-
?
additional information
?
-
-
cytochrome c3 is the natural electron acceptor
-
-
?
additional information
?
-
-
nonaheme cytochrome c is a competent physiological electron acceptor for the [Ni,Fe] hydrogenase
-
-
?
additional information
?
-
-
cytochrome c3 from Desulfovibrio vulgaris strain Hildenborough, enzyme forms an electron-transfer complex with cytochrome c3 for an electron shuttle between the periplasmic enzyme and the membrane-bound cytochrome c3
-
-
?
additional information
?
-
-
enzyme reduces soluble uranium(VI) with ferrocytochrome c3 as electron donor to uranium(IV) forming the insoluble mineral uraninite, this reaction is impaired in a cytochrome c3 mutant strain
-
-
?
additional information
?
-
-
the enzyme is associated to cytochrome c3, a tetraheme 13 kDa metalloprotein, analysis of electron binding, cooperativity effects, the Redox-Bohr effect, and thermodynamics of cytochrome c3
-
-
?
additional information
?
-
-
nonaheme cytochrome c is a competent physiological electron acceptor for the [Ni,Fe] hydrogenase
-
-
?
additional information
?
-
-
cytochrome c3 is the natural electron acceptor
-
-
?
additional information
?
-
-
enzyme reduces soluble uranium(VI) with ferrocytochrome c3 as electron donor to uranium(IV) forming the insoluble mineral uraninite, this reaction is impaired in a cytochrome c3 mutant strain
-
-
?
additional information
?
-
-
the enzyme catalyzes the conversion of para-H2 to normal H2 over D2O as well as the isotope exchange reaction in the H2D2O system
-
-
?
additional information
?
-
-
enzyme reduces soluble uranium(VI) with ferrocytochrome c3 as electron donor to uranium(IV) forming the insoluble mineral uraninite, this reaction is impaired in a cytochrome c3 mutant strain
-
-
?
additional information
?
-
-
the enzyme catalyzes the conversion of para-H2 to normal H2 over D2O as well as the isotope exchange reaction in the H2D2O system
-
-
?
additional information
?
-
Solidesulfovibrio fructosivorans
-
enzyme also exhibits high Tc(VII)-reducing activity
-
-
?
additional information
?
-
Solidesulfovibrio fructosivorans
-
cytochrome c3 is the natural electron acceptor
-
-
?
additional information
?
-
-
a natural electron donor is a low-potential c3 cytochrome
-
-
?
additional information
?
-
-
a natural electron donor is a low-potential c3 cytochrome
-
-
?
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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
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
the type I cytochrome C3 complex is more efficient than type II cytochrome c3 complex as electron acceptor from hydrogenase
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
part of an electron transport chain that mediates electronic coupling between periplasmic hydrogen oxidation and cytosolic sulfate reduction
-
-
r
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
part of an electron transport chain that mediates electronic coupling between periplasmic hydrogen oxidation and cytosolic sulfate reduction
-
-
r
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
-
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
-
-
?
additional information
?
-
-
cytochrome c3 is the natural electron acceptor
-
-
?
additional information
?
-
-
cytochrome c3 is the natural electron acceptor
-
-
?
additional information
?
-
-
nonaheme cytochrome c is a competent physiological electron acceptor for the [Ni,Fe] hydrogenase
-
-
?
additional information
?
-
-
nonaheme cytochrome c is a competent physiological electron acceptor for the [Ni,Fe] hydrogenase
-
-
?
additional information
?
-
-
cytochrome c3 is the natural electron acceptor
-
-
?
additional information
?
-
Solidesulfovibrio fructosivorans
-
cytochrome c3 is the natural electron acceptor
-
-
?
additional information
?
-
-
a natural electron donor is a low-potential c3 cytochrome
-
-
?
additional information
?
-
-
a natural electron donor is a low-potential c3 cytochrome
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochrome c
-
nonaheme cytochrome c is a competent physiological electron acceptor
iron-sulfur centre
Megalodesulfovibrio gigas
-
the active site of this protein is located in the large subunit, and the small subunit contains one [3Fe4S] and two [4Fe4S] iron-sulfur centres
cytochrome c3
Megalodesulfovibrio gigas
-
requires the presence of cytochrome c3 for the reduction of ferredoxin, rubredoxin and cytochrome c3
-
cytochrome c3
-
the electron transfer between [NiFeSe] hydrogenase and octaheme cytochrome c3 is activated by tetraheme cytochrome c3, cytochrome c3 can acts as an electron shuttle between hydrogenase and polyheme cytochromes
-
cytochrome c3
-
the electron transfer between [NiFeSe] hydrogenase and octaheme cytochrome c3 is activated by tetraheme cytochrome c3, cytochrome c3 can acts as an electron shuttle between hydrogenase and polyheme cytochromes
-
cytochrome c3
-
the enzyme is associated to cytochrome c3, a tetraheme 13 kDa metalloprotein, analysis of electron binding, cooperativity effects, the Redox-Bohr effect, and thermodynamics of cytochrome c3
-
cytochrome c3
-
hydrogen-dependent platinum (IV) reducing activity in the presence of hydrogenase and its physiological electron carrier, cytochrome c3. Reduction of platinum by the purified hydrogenase enzyme alone yields about 10% removal after 3 h incubation while after the addition of cytochrome c3 there is a slight increase to 15%. Suppression of enzyme activity due to the extreme acid pH of 0.38 of the effluent
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe
Iron
Ni
Nickel
Se
selenium