Study of the lipid-protein interaction of F ATPases.
Mg2+ may play a role in altering the lipid fluidity of the bilayers which would induce a change in conformation of the F0 portion of the H(+)-ATPase complex. This change could be transmitted to the soluble F1 portion, the conformation of which is in turn altered, resulting in higher enzymic activity. In addition to mitochondrial H(+)-ATPase, similar Mg2+ effects on the reconstitution of chloroplast H(+)-ATPase and other intrinsic membrane proteins have also been observed in our laboratory.
Yang
F Y
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National Laboratory of Biomacromolecules, Academia Sinica, Beijing, China.
D000818:Animals; D007700:Kinetics; D008051:Lipid Bilayers / Q000378:metabolism; D008081:Liposomes / Q000378:metabolism; D046911:Macromolecular Substances; D008274:Magnesium / Q000378:metabolism / Q000494:pharmacology; D008560:Membrane Fluidity; D008928:Mitochondria / Q000201:enzymology; D008961:Models, Structural; D011510:Proteolipids / Q000737:chemistry / Q000378:metabolism*; D006180:Proton-Translocating ATPases / Q000737:chemistry / Q000378:metabolism*
D008051:Lipid Bilayers; D008081:Liposomes; D046911:Macromolecular Substances; D011510:Proteolipids; C020485:proteoliposomes; D006180:Proton-Translocating ATPases; D008274:Magnesium