ATP合酶
ATP合成酶γ亚单位
化学渗透
ATP水解
电化学梯度
F-ATP酶
蛋白质亚单位
费斯特共振能量转移
化学
三磷酸腺苷
酶
生物物理学
生物化学
ATP酶
立体化学
膜
生物
荧光
叶绿体
类囊体
基因
量子力学
物理
作者
Manuel Diez,Boris Zimmermann,Michael Börsch,Marcelle König,Enno Schweinberger,Stefan Steigmiller,Rolf Reuter,Suren Felekyan,Volodymyr Kudryavtsev,Claus A. M. Seidel,Peter Gräber
摘要
Synthesis of ATP from ADP and phosphate, catalyzed by F0F1-ATP synthases, is the most abundant physiological reaction in almost any cell. F0F1-ATP synthases are membrane-bound enzymes that use the energy derived from an electrochemical proton gradient for ATP formation. We incorporated double-labeled F0F1-ATP synthases from Escherichia coli into liposomes and measured single-molecule fluorescence resonance energy transfer (FRET) during ATP synthesis and hydrolysis. The γ subunit rotates stepwise during proton transport–powered ATP synthesis, showing three distinct distances to the b subunits in repeating sequences. The average durations of these steps correspond to catalytic turnover times upon ATP synthesis as well as ATP hydrolysis. The direction of rotation during ATP synthesis is opposite to that of ATP hydrolysis.
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