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J Bacteriol. 1969 March; 97(3): 1001-1004
Copyright © 1969 American Society for Microbiology. All Rights Reserved.

Terminal Electron Transport in Leptospira

¹ Department of Microbiology, University of Massachusetts, Amherst, Massachusetts 01002

ABSTRACT

The cytochrome content of three leptospiral strains grown in several media was investigated after it was shown that respiratory inhibitors suppressed oxygen consumption of a water isolate, B₁₆, and that two pathogenic serotypes, pomona and schueffneri, were active catalase producers, whereas B₁₆ lacked catalase activity. Reduced minus oxidized difference spectra disclosed cytochromes of the a, c, and c₁ types in all strains. Although no spectral evidence suggested the existence of cytochrome b components, they could have been masked by cytochrome c, and their presence cannot be ruled out. Carbon monoxide difference spectra revealed peaks indicative of a cytochrome oxidase of the o type in all strains. Carbon monoxide spectra further suggested that a cytochrome a oxidase, possibly a₁ or a₃, and a pigment with absorption spectra different from those of previously characterized cytochromes existed in the two pathogens and not in the water isolate. Physiological reduction of the cytochromes by various metabolic substrates implied that the cytochrome system in Leptospira was functional. No effect of the various growth media on the cytochrome patterns of the three strains was observed, indicating that all three strains were capable of synthesis of cytochrome components and did not require heme prosthetic groups present in serum.