Interaction of ubiquinone and vitamin K3 with mitochondrial succinate-ubiquinone oxidoreductase.
Two new methods have been devised for measuring fumarate reduction by beef heart succinate-ubiquinone oxidoreductase with quinols as electron donors. In one assay the quinone is maintained in the reduced state by coupling fumarate reduction with the DT-diaphorase reaction, in the other assay by the presence of excess dithionite. The advantages of these methods are discussed, along with preliminary characterization of the quinol-protein interaction.
Kotlyar
A B
AB
Dept. of Biochemistry, Tel Aviv University, Ramat Aviv, Israel.
Gutman
M
M
Ackrell
B A
BA
D000818:Animals; D002417:Cattle; D004227:Dithionite / Q000494:pharmacology; D042963:Electron Transport Complex II; D007700:Kinetics; D008929:Mitochondria, Heart / Q000201:enzymology*; D009097:Multienzyme Complexes / Q000378:metabolism*; D016660:NAD(P)H Dehydrogenase (Quinone) / Q000378:metabolism; D010088:Oxidoreductases / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet; D013385:Succinate Dehydrogenase / Q000378:metabolism*; D014451:Ubiquinone / Q000378:metabolism*; D014812:Vitamin K / Q000378:metabolism*
D009097:Multienzyme Complexes; D014812:Vitamin K; D014451:Ubiquinone; D004227:Dithionite; D010088:Oxidoreductases; D042963:Electron Transport Complex II; D013385:Succinate Dehydrogenase; D016660:NAD(P)H Dehydrogenase (Quinone)