Chemical modification of active sites in relation to the catalytic mechanism of F1.
Recent studies of chemically modified F1-ATPases have provided new information that requires a revision of our thinking on their catalytic mechanism. One of the beta subunits in F1-ATPase is distinguishable from the other two both structurally and functionally. The catalytic site and regulatory site of the same beta subunit are probably sufficiently close to each other, and the interaction between the various catalytic and regulatory sites are probably sufficiently strong to raise the uni-site rate of ATP hydrolysis by several orders of magnitude to that of promoted (multi-site) ATP hydrolysis. Although all three beta subunits in F1 possess weak uni-site ATPase activity, only one of them (beta') catalyzes promoted ATP hydrolysis. But all three beta subunits catalyze ATP synthesis driven by the proton flux. Internal rotation of the alpha 3beta 3 or beta 3 moiety relative to the remainder of the F0F1 complex did not occur during oxidative phosphorylation by reconstituted submitochondrial particles.
Wang
J H
JH
Bioenergetics Laboratory, State University of New York, Buffalo 14214-3094.
D001665:Binding Sites; D002384:Catalysis; D008962:Models, Theoretical; D011485:Protein Binding; D006180:Proton-Translocating ATPases / Q000378:metabolism*
D006180:Proton-Translocating ATPases