alpha, beta-Bidentate CrADP abolishes the negative cooperativity of yeast mitochondrial F1-ATPase.
The hydrolysis of MgATP and MgITP by mitochondrial F1-ATPase from Saccharomyces cerevisiae is competitively inhibited by alpha, beta-CrADP, alpha, beta, gamma-CrATP and beta, gamma-CrATP. The apparent K1 values of the three complexes are in the range of the half-saturating MgATP concentration. The negative cooperativity (nH = 0.7) of MgATP hydrolysis is totally abolished by alpha, beta-CrADP (nH = 1.0), while it is not affected by the CrATP. It is concluded that alpha, beta-CrADP binds exclusively at the regulatory site and that CrATP binds exclusively to the catalytic site.
Wieker
H J
HJ
Hess
B
B
D000244:Adenosine Diphosphate / Q000378:metabolism / Q000494:pharmacology*; D000255:Adenosine Triphosphate / Q000378:metabolism / Q000494:pharmacology; D007293:Inosine Triphosphate / Q000378:metabolism; D007700:Kinetics; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013237:Stereoisomerism
D007293:Inosine Triphosphate; C036863:magnesium ITP; D000244:Adenosine Diphosphate; C007144:chromium adenosine diphosphate; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases