Information on EC 1.12.5.1 - hydrogen:quinone oxidoreductase

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hydrogen:menaquinone oxidoreductase

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Hydrogen:quinone oxidoreductase

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hydrogenase (Wolinella succinogenes clone pHyd1 gene hydA subunit precursor reduced)

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hydrogenase (Wolinella succinogenes clone pHyd1 gene hydB subunit precursor reduced)

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hydrogenase (Wolinella succinogenes clone pHyd1 gene hydC subunit)

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147097-27-6

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147097-28-7

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147097-29-8

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151616-65-8

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expresses hydrogenase constitutively

Bradyrhizobium japonicum SR473

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expresses hydrogenase constitutively

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394192, 394193, 676044

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H2 + 2,3-dimethyl-1,4-naphthoquinone

reduced 2,3-dimethyl-1,4-naphthoquinone

3 entries

H2 + benzyl viologen

reduced benzyl viologen

3 entries

H2 + menaquinone

menaquinol

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?

cytochrome c

2 entries

heme

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the cytochrome b subunit of Wolinella succinogenes hydrogenase binds two heme B groups, HydABC contains 0.0121 mM heme per g of protein

Fe

2 entries

Ni

2 entries

2-n-heptyl-4-hydroxyquinoline-N-oxide

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0.1 mM, 17% inhibition

antimycin A

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0.1 mM, 47% inhibition

505

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7.9

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cytoplasmic membrane

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3ayx, download, 3D-view

SCOPe (3ayx)

CATH (3ayx)

Hydrogenovibrio marinus

F2Z6J6

3ayz, download, 3D-view

SCOPe (3ayz)

CATH (3ayz)

Hydrogenovibrio marinus

F2Z6J6

5y34, download, 3D-view

SCOPe (5y34)

CATH (5y34)

Hydrogenovibrio marinus

F2Z6J6

23000

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x * 23000, cytochrome b, + x * 30000 + x * 60000, SDS-PAGE

394192

26828

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x * 26828, HydC, + x * 31968, HydA, + x * 63866, HydB, calculation from nucleotide sequence

30000

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x * 23000, cytochrome b, + x * 30000 + x * 60000, SDS-PAGE

394192

31968

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x * 26828, HydC, + x * 31968, HydA, + x * 63866, HydB, calculation from nucleotide sequence

33000

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1 * 65000 + 1 * 33000

60000

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x * 23000, cytochrome b, + x * 30000 + x * 60000, SDS-PAGE

394192

63866

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x * 26828, HydC, + x * 31968, HydA, + x * 63866, HydB, calculation from nucleotide sequence

65000

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1 * 65000 + 1 * 33000

82600

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gel filtration

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dimer

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H122A

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mutation in HydC subunit results in an enzyme with wild-type properties

H158A

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mutation in HydC subunit results in an enzyme with wild-type properties

H186A

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mutation in the HydC subunit causes the loss of quinone reactivity of the hydrogenase, while the activity of benzylviologen reduction is retained. The corresponding mutants do not grow with H2 as electron donor and either fumarate or polysulfide as terminal electron acceptor. The mutants grown with formate and fumarate do not catalyse electron transport from H2 to fumarate or to polysulfide, or quinone reduction by H2, in contrast to the wild-type strain. Cytochrome b is not reduced by H2 in the Triton X-100 extract of the mutant membranes, which contains wild-type amounts of the mutated HydC protein

H186M

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mutation in the HydC subunit causes the loss of quinone reactivity of the hydrogenase, while the activity of benzylviologen reduction is retained. The corresponding mutants do not grow with H2 as electron donor and either fumarate or polysulfide as terminal electron acceptor. The mutants grown with formate and fumarate do not catalyse electron transport from H2 to fumarate or to polysulfide, or quinone reduction by H2, in contrast to the wild-type strain. Cytochrome b is not reduced by H2 in the Triton X-100 extract of the mutant membranes, which contains wild-type amounts of the mutated HydC protein

H187A

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mutation in HydC subunit results in an enzyme with wild-type properties

H188A

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mutation in hydA subuni causes loss of quinone reactivity of the hydrogenase, while the activity of benzylviologen reduction is retained. The corresponding mutants do not grow with H2 as electron donor and either fumarate or polysulfide as terminal electron acceptor. The mutants grown with formate and fumarate do not catalyse electron transport from H2 to fumarate or to polysulfide, or quinone reduction by H2, in contrast to the wild-type strain. Cytochrome b is not reduced by H2 in the Triton X-100 extract of the mutant membranes, which contains wild-type amounts of the mutated HydC protein

H25A

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mutation in the HydC subunit causes the loss of quinone reactivity of the hydrogenase, while the activity of benzylviologen reduction is retained. The corresponding mutants do not grow with H2 as electron donor and either fumarate or polysulfide as terminal electron acceptor. The mutants grown with formate and fumarate do not catalyse electron transport from H2 to fumarate or to polysulfide, or quinone reduction by H2, in contrast to the wild-type strain. Cytochrome b is not reduced by H2 in the Triton X-100 extract of the mutant membranes, which contains wild-type amounts of the mutated HydC protein

H25M

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mutation in the HydC subunit causes the loss of quinone reactivity of the hydrogenase, while the activity of benzylviologen reduction is retained. The corresponding mutants do not grow with H2 as electron donor and either fumarate or polysulfide as terminal electron acceptor. The mutants grown with formate and fumarate do not catalyse electron transport from H2 to fumarate or to polysulfide, or quinone reduction by H2, in contrast to the wild-type strain. Cytochrome b is not reduced by H2 in the Triton X-100 extract of the mutant membranes, which contains wild-type amounts of the mutated HydC protein

H305M

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mutation in hydA subuni causes loss of quinone reactivity of the hydrogenase, while the activity of benzylviologen reduction is retained. The corresponding mutants do not grow with H2 as electron donor and either fumarate or polysulfide as terminal electron acceptor. The mutants grown with formate and fumarate do not catalyse electron transport from H2 to fumarate or to polysulfide, or quinone reduction by H2, in contrast to the wild-type strain. Cytochrome b is not reduced by H2 in the Triton X-100 extract of the mutant membranes, which contains wild-type amounts of the mutated HydC protein

H67A

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mutation in the HydC subunit causes the loss of quinone reactivity of the hydrogenase, while the activity of benzylviologen reduction is retained. The corresponding mutants do not grow with H2 as electron donor and either fumarate or polysulfide as terminal electron acceptor. The mutants grown with formate and fumarate do not catalyse electron transport from H2 to fumarate or to polysulfide, or quinone reduction by H2, in contrast to the wild-type strain. Cytochrome b is not reduced by H2 in the Triton X-100 extract of the mutant membranes, which contains wild-type amounts of the mutated HydC protein

H67M

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mutation in the HydC subunit causes the loss of quinone reactivity of the hydrogenase, while the activity of benzylviologen reduction is retained. The corresponding mutants do not grow with H2 as electron donor and either fumarate or polysulfide as terminal electron acceptor. The mutants grown with formate and fumarate do not catalyse electron transport from H2 to fumarate or to polysulfide, or quinone reduction by H2, in contrast to the wild-type strain. Cytochrome b is not reduced by H2 in the Triton X-100 extract of the mutant membranes, which contains wild-type amounts of the mutated HydC protein