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SYSTEMATIC NAME
IUBMB Comments
hydrogen:quinone oxidoreductase
Contains nickel, iron-sulfur clusters and cytochrome b. Also catalyses the reduction of water-soluble quinones (e.g. 2,3-dimethylnaphthoquinone) or viologen dyes (benzylviologen or methylviologen).
x * 23000, cytochrome b, + x * 30000 + x * 60000, SDS-PAGE; x * 26828, HydC, + x * 31968, HydA, + x * 63866, HydB, calculation from nucleotide sequence
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
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
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
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
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
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
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
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