1.12.5.1: hydrogen:quinone oxidoreductase

This is an abbreviated version!
For detailed information about hydrogen:quinone oxidoreductase, go to the full flat file.

Word Map on EC 1.12.5.1

Reaction

H2
+
menaquinone
=
menaquinol

Synonyms

EC 1.12.99.3, HydABC, hydrogen:menaquinone oxidoreductase, Hydrogen:quinone oxidoreductase, hydrogenase (Wolinella succinogenes clone pHyd1 gene hydA subunit precursor reduced), hydrogenase (Wolinella succinogenes clone pHyd1 gene hydB subunit precursor reduced), hydrogenase (Wolinella succinogenes clone pHyd1 gene hydC subunit)

ECTree

     1 Oxidoreductases
         1.12 Acting on hydrogen as donor
             1.12.5 With a quinone or similar compound as acceptor
                1.12.5.1 hydrogen:quinone oxidoreductase

Engineering

Engineering on EC 1.12.5.1 - hydrogen:quinone oxidoreductase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H122A
-
mutation in HydC subunit results in an enzyme with wild-type properties
H158A
-
mutation in HydC subunit results in an enzyme with wild-type properties
H186A
-
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
-
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
-
mutation in HydC subunit results in an enzyme with wild-type properties
H188A
-
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
-
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
-
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
-
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
-
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
-
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