Literature summary for 1.12.5.1 extracted from

Gross, R.; Simon, J.; Lancaster, R.D.; Kr�ger, A.
Identification of histidine residues in Wolinella succinogenes hydrogenase that are essential for menaquinone reduction by H2 (1998), Mol. Microbiol., 30, 639-646.

Search for more literature for 1.12.5.1

Protein Variants

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

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

Organism

Organism	UniProt	Comment	Textmining
Wolinella succinogenes	-	-	-

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
HydABC	-	Wolinella succinogenes

Cofactor

Cofactor	Comment	Organism	Structure
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

Organism	Comment	pI Value Maximum	pI Value
Wolinella succinogenes	-	-	7.9

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Release 2023.1 (January 2023)