title: The Possible Role of Nonbilayer Structures in Regulating ATP Synthase Activity in Mitochondrial Membranes.
abstract: The effects of temperature and of the membrane-active protein CTII on the formation of nonbilayer structures in mitochondrial membranes were studied by31P-NMR. Increasing the temperature of isolated mitochondrial fractions correlated with an increase in ATP synthase activity and the formation of nonbilayer packed phospholipids with immobilized molecular mobility. Computer modeling was employed for analyzing the interaction of mitochondrial membrane phospholipids with the molecular surface of CTII, which behaves like a dicyclohexylcarbodiimide-binding protein (DCCD-BP) of the F0group in a lipid phase. Overall, our studies suggest that proton permeability toroidal pores formed in mitochondrial membranes consist of immobilized nonbilayer-packed phospholipids formed via interactions with DCCD-BP. Our studies support the existence of a proton transport along a concentration gradient mediated via transit toroidal permeability pores which induce conformational changes necessary for mediating the catalytic activity of ATP synthase in the subunits of the F0-F1complex.
authors.affiliation: Moscow State University Branch, 22a A. Timur Avenue, Tashkent, 100060 Uzbekistan.
authors.forename: S E
authors.initials: SE
authors.lastname: Gasanov
authors.affiliation: Moscow State University Branch, 22a A. Timur Avenue, Tashkent, 100060 Uzbekistan.
authors.forename: A A
authors.initials: AA
authors.lastname: Kim
authors.affiliation: Department of Pharmacology, University of Nevada, Reno School of Medicine,1664 North Virginia St., Reno, Nevada, 89557 United States.
authors.forename: R K
authors.initials: RK
authors.lastname: Dagda