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The possible role of nonbilayer structures in regulating ATP synthase activity in mitochondrial membranes
Biophysics Pub Date : 2016-07-01 , DOI: 10.1134/s0006350916040084
S E Gasanov 1 , A A Kim 1 , R K Dagda 2
Affiliation  

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.

中文翻译:

非双层结构在调节线粒体膜中 ATP 合酶活性中的可能作用

通过31P-NMR研究了温度和膜活性蛋白CTII对线粒体膜非双层结构形成的影响。首次发现 ATP 合酶活性的增加伴随着线粒体膜中具有固定分子移动性的非双层包装磷脂的形成。计算机建模还用于研究线粒体膜中发现的重要磷脂与 CTII 分子表面的相互作用,CTII 的行为类似于脂质相中 F0 基团的二环己基碳二亚胺结合蛋白 (DCCD-BP)。质子通透性环形孔被假定为通过与 DCCD-BP 相互作用固定的非双层包装磷脂在线粒体膜中形成。
更新日期:2016-07-01
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