Mitochondrial mbrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the mbrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extrambraneous catalytic core, and F0 - containing the mbrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Modulation of F0F1-ATP synthase activity by cyclophilin D regulates matrix adenine nucleotide levels.Chinopoulos C., Konrad C., Kiss G., Metelkin E., Torocsik B., Zhang S.F., Starkov A.A.FEBS J. 278:1112-1125(2011)
Research Topic:Others
