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J Bacteriol. 1961 December; 82(6): 927-932
Copyright © 1961, The Williams & Wilkins Company. All Rights Reserved.

STUDIES ON THERMOPHILIC SULFATE-REDUCING BACTERIA II.

Hydrogenase Activity of Clostridium nigrificans1

J. M. Akagi2 and L. Leon Campbell3

a Department of Microbiology, School of Medicine, Western Reserve University, Cleveland, Ohio

ABSTRACT

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 H2 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 H2 utilization. In contrast, Fe++ ions were not required to catalyze the evolution of H2 from reduced methyl viologen. The role of Fe++ ions in the hydrogenase activity of this organism is discussed.

FOOTNOTES

2 Post-Doctoral Research Fellow. Present address: Department of Bacteriology, University of Kansas, Lawrence.

3 Senior Research Fellow of the U. S. Public Health Service (SF 315).

1 This study was supported in part by grant E-2646 from the National Institute of Allergy and Infectious Diseases, U. S. Public Health Service. Presented at the 61st Annual Meeting of the American Society for Microbiology, Chicago, Ill., April 23–27, 1961.

J Bacteriol. 1961 December; 82(6): 927-932
Copyright © 1961, The Williams & Wilkins Company. All Rights Reserved.





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