Studies on thermophilic sulfate-reducing bacteria. II. Hydrogenase activity of Clostridium nigrificans.
Akagi, J. M. (Western Reserve University, Cleveland, Ohio) and L. Leon Campbell. Studies on thermophilic sulfate-reducing bacteria. II. Hydrogenase activity of Clostridium nigrificans. J. Bacteriol. 82:927-932. 1961.-The hydrogenase of Clostridium nigrificans has been found to be associated with the cell-free particulate fraction which can be sedimented at 105,000 x g in 1 hr. The specific activity of this fraction was increased 2 to 3 fold over that of the crude extract. It was not found possible to liberate the enzyme from the particulate fraction by methods of enzymatic digestion, chemical extraction, or physical disruption. The optimum temperature for H(2) utilization using benzyl viologen as an electron acceptor was found to be 55 C, and the optimum pH range was 7 to 8. Employing metal complexing agents it was found that the enzyme required Fe(++) ions for H(2) utilization. In contrast, Fe(++) ions were not required to catalyze the evolution of H(2) from reduced methyl viologen. The role of Fe(++) ions in the hydrogenase activity of this organism is discussed.
D001105:Archaea; D001419:Bacteria; D001594:Benzyl Viologen; D002384:Catalysis; D003013:Clostridium; D006864:Hydrogenase; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000378:metabolism*; D010269:Paraquat; D013431:Sulfates
D013431:Sulfates; D001594:Benzyl Viologen; D010088:Oxidoreductases; D006864:Hydrogenase; D010269:Paraquat
DEHYDROGENASES/metabolism