Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
TreeGrafter-generated GO annotations
Combined Automated Annotation using Multiple IEA Methods
[NiFe] hydrogenase from Desulfovibrio desulfuricans ATCC 27774: gene sequencing, three-dimensional structure determination and refinement at 1.8 A and modelling studies of its interaction with the tetrahaem cytochrome c3.
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The crystal structure of the [NiFe] hydrogenase of this strain was determined at 1.8 A, showing the iron-sulfur cluster chain of the small subunit running up to the [NiFe] centre of the large subunit.
"has been modified [4Fe-3S-3O] by loss of one sulfur atom and inclusion of three oxygen atoms"
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The physiological electron acceptor is the tetrahaem cytochrome c3 of the same organism, which docks at the distal [4Fe-4S] cluster of the small subunit.
"an interaction between the haem IV region in tetrahaem cytochrome c3 with the distal [4Fe-4S] cluster"
Identification of three classes of hydrogenase in the genus, Desulfovibrio.
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Amino-terminal sequencing of large and small subunits distinguishes the iron, iron+nickel and iron+nickel+selenium hydrogenase classes of Desulfovibrio; this work determined residues 50-67 of the mature small subunit of the ATCC 27774 enzyme.
"A comparison of amino-terminal amino acid sequences from the large and small subunits of hydrogenases from Desulfovibrio reveals significant differences."
Enzymatic recovery of elemental palladium by using sulfate-reducing bacteria.
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H2-dependent reduction of Pd(II) to cell-surface Pd(0) by resting Desulfovibrio desulfuricans cells was attributed to hydrogenase activity on the basis of H2 dependence and Cu2+ sensitivity, without genetic confirmation.
"the lack of molecular genetic studies on D. desulfuricans makes confirmation with specific deletion mutants difficult, but the involvement of hydrogenase activity is strongly implicated"
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Metal reduction in this organism is localised to the periplasm, the compartment in which this hydrogenase operates.
"the site of metal reduction and precipitation is the periplasm"
Bioaccumulation of palladium by Desulfovibrio fructosivorans wild-type and hydrogenase-deficient strains.
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Hydrogenase mutants of a different Desulfovibrio species still reduced Pd(II), with nanoparticle location tracking the remaining hydrogenase, so no single hydrogenase is established as necessary for Pd(0) deposition.
"Wild-type Desulfovibrio fructosivorans and three hydrogenase-negative mutants reduced Pd(II) to Pd(0)."