Purification and properties of a hydrogenase from Desulfovibrio vulgaris.

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 c(3) was studied. Metal analysis of the hydrogenase indicated the presence of 1 mole of ferrous iron per mole of enzyme.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Haschke RH,Campbell LL

doi

10.1128/JB.105.1.249-258.1971

subject

Has Abstract

pub_date

1971-01-01 00:00:00

pages

249-58

issue

1

eissn

0021-9193

issn

1098-5530

journal_volume

105

pub_type

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