NADH-linked fumarate reductase and NADH dehydrogenase activities in Fibrobacter succinogenes

Crude membrane preparations from Fibrobacter succinogenes S85 were investigated and found to contain NADH dehydrogenase (NADH:decylubiquinone oxidoreductase) and NADH-linked fumarate reductase activities. Under aerobic conditions the maximum NADH dehydrogenase activity (252 nmoles/min/mg protein) wa...

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Bibliographic Details
Published in:Current microbiology 1994-04, Vol.28 (4), p.247-251
Main Authors: MEINHARDT, S. W, GLASS, T. L
Format: Article
Language:English
Subjects:
Bacteriology
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Metabolism. Enzymes
Microbiology
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Summary:Crude membrane preparations from Fibrobacter succinogenes S85 were investigated and found to contain NADH dehydrogenase (NADH:decylubiquinone oxidoreductase) and NADH-linked fumarate reductase activities. Under aerobic conditions the maximum NADH dehydrogenase activity (252 nmoles/min/mg protein) was ten times greater than that of NADH-fumarate reductase (23 nmoles/min/mg protein). NADH-fumarate reductase was strongly inhibited by 2-heptyl-4-hydroxyquinoline-N-oxide (HOQNO), rotenone, HgCl sub(2), and o-phenanthroline. Inhibition of the NADH dehydrogenase by the first three compounds, particularly rotenone, accounted for most of the effects on NADH-fumarate reductase. The alpha -band of a b-type cytochrome was resolved into two cytochromes, a cytochrome b sub(560) (oxidized by addition of HOQNO) and a cytochrome b sub(563) (oxidized by subsequent addition of fumarate).
ISSN:0343-8651
1432-0991
DOI:10.1007/BF01575969