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Literature summary extracted from

  • Gross, R.; Simon, J.; Lancaster, R.D.; Kr๖ger, A.
    Identification of histidine residues in Wolinella succinogenes hydrogenase that are essential for menaquinone reduction by H2 (1998), Mol. Microbiol., 30, 639-646.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.12.5.1 H122A mutation in HydC subunit results in an enzyme with wild-type properties Wolinella succinogenes
1.12.5.1 H158A mutation in HydC subunit results in an enzyme with wild-type properties Wolinella succinogenes
1.12.5.1 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 Wolinella succinogenes
1.12.5.1 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 Wolinella succinogenes
1.12.5.1 H187A mutation in HydC subunit results in an enzyme with wild-type properties Wolinella succinogenes
1.12.5.1 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 Wolinella succinogenes
1.12.5.1 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 Wolinella succinogenes
1.12.5.1 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 Wolinella succinogenes
1.12.5.1 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 Wolinella succinogenes
1.12.5.1 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 Wolinella succinogenes
1.12.5.1 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 Wolinella succinogenes

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.12.5.1 Fe the enzyme contain 0.096 mM Fe per g of enzyme Wolinella succinogenes
1.12.5.1 Ni contains 0.0077 mM Ni per g of enzyme Wolinella succinogenes

Organism

EC Number Organism UniProt Comment Textmining
1.12.5.1 Wolinella succinogenes
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.12.5.1 H2 + 2,3-dimethyl-1,4-naphthoquinone
-
 Wolinella succinogenes reduced 2,3-dimethyl-1,4-naphthoquinone
-
 ?
1.12.5.1 H2 + benzyl viologen
-
 Wolinella succinogenes reduced benzyl viologen
-
 ?
1.12.5.1 H2 + menaquinone
-
 Wolinella succinogenes menaquinol
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.12.5.1 HydABC
-
 Wolinella succinogenes

Cofactor

EC Number Cofactor Comment Organism Structure
1.12.5.1 heme the cytochrome b subunit of Wolinella succinogenes hydrogenase binds two heme B groups, HydABC contains 0.0121 mM heme per g of protein Wolinella succinogenes

pI Value

EC Number Organism Comment pI Value Maximum pI Value
1.12.5.1 Wolinella succinogenes
-
-
 7.9