1887

Abstract

Summary: Active, membrane-bound NADH and succinate oxidase activities with a temperature optimum of 75 °C were demonstrated in an extremely thermophilic bacterium. These were relatively stable in cell-free extracts and respiratory particles at 75 °C, but at 90 °C the half-lives of these oxidase systems were about 15 min in respiratory particles and 80 min in cell-free extracts. The stability of the NADH oxidase in respiratory particles at 90 °C was enhanced by 2 -(NH)SO, 50% (v/v) glycerol and by NADH. A number of other substrates were oxidized by the electron transport system. Respiratory particles contained cytochromes -613, -602, -559, cytochrome and at least one -type cytochrome, -555. The soluble fraction contained at least two -type cytochromes, at least one of which was CO-reactive. The sensitivity of NADH and succinate oxidases to a range of inhibitors was determined.

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1979-09-01
2021-05-09
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