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. 1971 Jan;105(1):249–258. doi: 10.1128/jb.105.1.249-258.1971

Purification and Properties of a Hydrogenase from Desulfovibrio vulgaris1

Richard H Haschke a, L Leon Campbell a
PMCID: PMC248348  PMID: 5541010

Abstract

The soluble hydrogenase of Desulfovibrio vulgaris was purified and some of its properties are described. The molecular weight was determined for the enzyme by sedimentation equilibrium (45,400) and amino acid analysis (44,800). The hydrogenase appears to be a loosely coiled molecule or to have a high axial ratio, which is reflected in an unusually low sedimentation coefficient (2.58S) and a low diffusion coefficient (D 5.85). The molecular weight of the hydrogenase (41,000), as calculated by the Svedberg equation, was in general agreement with the sedimentation equilibrium molecular weight. Amino acid analysis revealed the presence of six halfcystine residues per mole of enzyme and a total of 417 amino acid residues. The specificity of the hydrogenase and its capacity to reduce certain low potential dyes and cytochrome c3 was studied. Metal analysis of the hydrogenase indicated the presence of 1 mole of ferrous iron per mole of enzyme.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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