The possible role of nonbilayer structures in regulating ATP synthase activity in mitochondrial membranes

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• 作者：S. E. Gasanov ; A. A. Kim ; R. K. Dagda
• 关键词：31P ; NMR ; mitochondrial membrane phospholipids ; ATP synthase
• 刊名：Biophysics
• 出版年：2016
• 出版时间：July 2016
• 年：2016
• 卷：61
• 期：4
• 页码：596-600
• 全文大小：844 KB
• 刊物主题：Biophysics and Biological Physics;
• 出版者：Springer US
• ISSN：1555-6654
• 卷排序：61

文摘

The effects of temperature and the membrane-active protein CTII on the formation of nonbilayer structures in mitochondrial membranes were studied by 31P-NMR. An increase in ATP synthase activity was found for the first time to accompany the formation of nonbilayer packed phospholipids with immobilized molecular mobility in mitochondrial membranes. Computer modeling was additionally employed in studying the interaction of important phospholipids found in mitochondrial membranes with the molecular surface of CTII, which behaves like a dicyclohexylcarbodiimide-binding protein (DCCD-BP) of the F₀ group in a lipid phase. Proton permeability toroidal pores were assumed to form in mitochondrial membranes from nonbilayer-packed phospholipids immobilized via interactions with DCCD-BP. Proton transport along a concentration gradient through the transit toroidal permeability pores may induce conformational changes necessary for mediating the catalytic activity of ATP synthase in the subunits of the F₀–F₁ complex.