Abstract
The membrane-bound hydrogenase [EC 1.12.-.-l ofEscherichia coli is involved in the energy-conserving oxidation of hydrogen [l-4] via fumarate reductase [EC 1.3.99.11 and also in the formate hydrogenlyase pathway which converts formate to COZ and Hz [5]. E. coli hydrogenase from aerobically grown cells has been isolated and characterised [6] and the enzyme from anaerobically grown cells has been partially characterised [7]. Antibodies specific for Bacillus subtilis membrane-bound succinate dehydrogenase [EC 1.3.99.11 have been raised from activity-stained precipitin arcs located after analysis of crude fractions by crossed immunoelectrophoresis using antisera raised to detergent-solubilised membranes [8]. We have used a similar approach to prepare antibodies specific for E. coli hydrogenase and its use has enabled the subunit MW of the enzyme from anaerobically grown cells to be determined. We also report the isolation and immunological characterisation of two new E. coli mutants which specifically lack hydrogenase activity.
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