Effect of physiological electron donors and acceptors on F1-ATPase.
The hydrolytic activity of F1-ATPase isolated from rat liver was enhanced in the presence of NADH, FADH2, QH2 or reduced cyt c. The extent of this activation depended largely on substrate concentration. F1-ATPase sensitivity to bicarbonate or dinitrophenol activators decreased in the presence of any of those electron donors, which originated as well a slight sensitivity to oligomycin and a sensitivity increase to the inhibitory anion OCN-. In the presence of oxidized carriers the sensitivity to bicarbonate, dinitrophenol, or OCN- was not modified, and the enzyme remained oligomycin insensitive.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D003485:Cyanates / Q000494:pharmacology; D003574:Cytochrome c Group / Q000378:metabolism; D004140:Dinitrophenols / Q000494:pharmacology; D004789:Enzyme Activation; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism; D008930:Mitochondria, Liver / Q000201:enzymology; D009243:NAD / Q000378:metabolism; D009840:Oligomycins / Q000494:pharmacology; D006180:Proton-Translocating ATPases; D051381:Rats; D014451:Ubiquinone / Q000378:metabolism
D003485:Cyanates; D003574:Cytochrome c Group; D004140:Dinitrophenols; D009840:Oligomycins; D009243:NAD; D014451:Ubiquinone; D005182:Flavin-Adenine Dinucleotide; D000251:Adenosine Triphosphatases; D006180:Proton-Translocating ATPases; C024835:potassium cyanate