NADH-linked fumarate reductase and NADH dehydrogenase activities inFibrobacter succinogenes
Copyright policy )NADH-linked fumarate reductase and NADH dehydrogenase activities inFibrobacter succinogenes
Crude membrane preparation fromFibrobacter 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, HgCl2, ando-phenanthroline. Inhibition of the NADH dehydrogenase by the first three compounds, particularly rotenone, accounted for most of the effects on NADH-fumarate reductase. The α-band of ab-type cytochrome was resolved into two cytochromes, a cytochromeb 560 (oxidized by addition of HOQNO) and a cytochromeb 563 (oxidized by subsequent addition of fumarate).
- North Dakota State University United States
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