Fixing the Q cycle

被引:168
作者
Osyczka, A [1 ]
Moser, CC [1 ]
Dutton, PL [1 ]
机构
[1] Univ Penn, Dept Biochem & Biophys, Johnson Res Fdn, Philadelphia, PA 19104 USA
关键词
D O I
10.1016/j.tibs.2005.02.001
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Mitchell ' s key insight that all bioenergetic membranes run on the conversion of redox energy into transmembrane electrical and proton gradients took the form 30 years ago of a working model of the Q cycle of cytochrome bc(1), which operates reversibly on coupled electron and proton transfers of quinone at two binding sites on opposite membrane faces. His remarkable model still stands today, but he had no structural information to provide understanding into how dangerous short-circuit redox reactions were avoided. Now, it is clear that the Q cycle must be fixed with a special mechanism that avoids serniquinone-mediated short circuits. Either the redox states of the quinone electron-transfer partners double-gate the semiquinone-intermediate stability, or serniquinone is avoided altogether in concerted double-electron transfer.
引用
收藏
页码:176 / 182
页数:7
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