F₀F₁-ATP合酶中质子驱动的c环旋转的36度步长。
36 degrees step size of proton-driven c-ring rotation in FoF1-ATP synthase.
作者信息
Düser Monika G, Zarrabi Nawid, Cipriano Daniel J, Ernst Stefan, Glick Gary D, Dunn Stanley D, Börsch Michael
机构信息
3. Physikalisches Institut, Universität Stuttgart, Stuttgart, Germany.
出版信息
EMBO J. 2009 Sep 16;28(18):2689-96. doi: 10.1038/emboj.2009.213. Epub 2009 Jul 30.
Abstract
Synthesis of adenosine triphosphate ATP, the 'biological energy currency', is accomplished by F(o)F(1)-ATP synthase. In the plasma membrane of Escherichia coli, proton-driven rotation of a ring of 10 c subunits in the F(o) motor powers catalysis in the F(1) motor. Although F(1) uses 120 degrees stepping during ATP synthesis, models of F(o) predict either an incremental rotation of c subunits in 36 degrees steps or larger step sizes comprising several fast substeps. Using single-molecule fluorescence resonance energy transfer, we provide the first experimental determination of a 36 degrees sequential stepping mode of the c-ring during ATP synthesis.
摘要
三磷酸腺苷（ATP），即“生物能量货币”，是由F(o)F(1)-ATP合酶合成的。在大肠杆菌的质膜中，F(o)马达中由质子驱动的10个c亚基环的旋转为F(1)马达中的催化作用提供动力。尽管F(1)在ATP合成过程中采用120度步幅，但F(o)模型预测c亚基要么以36度步幅进行增量旋转，要么以包含几个快速子步幅的更大步幅旋转。我们使用单分子荧光共振能量转移技术，首次通过实验确定了ATP合成过程中c环以36度顺序步幅的旋转模式。
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