Subunit movement in individual H+-ATP synthases during ATP synthesis and hydrolysis revealed by fluorescence resonance energy transfer.
Subunit movement in individual H+-ATP synthases during ATP synthesis and hydrolysis revealed by fluorescence resonance energy transfer.
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荧光共振能量转移揭示了 ATP 合成和水解过程中单个 H-ATP 合酶的亚基运动。
DOI：
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发表时间：
2005
影响因子：
3.9
通讯作者：
P. Gräber
中科院分区：
文献类型：
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作者：
M. Börsch;P. Gräber
F型H+-ATP合酶利用质子跨膜电化学势差提供的能量从ADP和磷酸盐合成ATP。酶内的旋转亚基运动分别驱动 ATP 水解或 ATP 合成方向的催化作用。为了以亚纳米分辨率实时监测这些亚基运动和相关构象变化，使用来自大肠杆菌的双标记 H+-ATP 合酶开发了单分子 FRET（荧光共振能量转移）方法。重组为脂质体后，当膜通电时，该酶能够催化 ATP 合成。
F-type H+-ATP synthases synthesize ATP from ADP and phosphate using the energy supplied by a transmembrane electrochemical potential difference of protons. Rotary subunit movements within the enzyme drive catalysis in either an ATP hydrolysis or an ATP synthesis direction respectively. To monitor these subunit movements and associated conformational changes in real time and with subnanometre resolution, a single-molecule FRET (fluorescence resonance energy transfer) approach has been developed using the double-labelled H+-ATP synthase from Escherichia coli. After reconstitution into a liposome, this enzyme was able to catalyse ATP synthesis when the membrane was energized.
DOI：
10.1073/pnas.92.24.10964
发表时间：
1995-11-21
影响因子：
11.1
作者：
DUNCAN, TM;BULYGIN, VV;CROSS, RL
通讯作者：
CROSS, RL