Electron microscopy of the F1F0 ATP synthase: From structure to function
Electron microscopy of the F1F0 ATP synthase: From structure to function
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F1F0 ATP 合酶的电子显微镜:从结构到功能
DOI:
--
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发表时间:
1994
期刊:
影响因子:
--
通讯作者:
E. Gogol
中科院分区:
文献类型:
--
作者:
E. Gogol
The 1F0 ATP synthase is the large multisubunit complex which uses the proton gradient of energetically active membranes to synthesize ATP. While biochemical and genetic approaches have characterized the composition of the enzyme and elucidated many details of its mechanism and assembly, electron microscopy has been the tool of primary importance in determining the arrangement of the many subunits which comprise the F1F0. The highly cooperative catalytic mechanism is tightly coupled to transmembrane proton translocation in a separate and rather distant sector of the complex. An understanding of this intricate process and its control requires an appreciation of subunit interactions, starting with their locations relative to one another. Electron microscopy has provided most of the available structural information on the F1F0, and recent applications of cryo‐electron microscopy have captured different functionally relevant configurations which may finally address longstanding questions about subunit rearrangement during the catalytic cycle. © 1994 Wiley‐Liss, Inc.
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DOI:
10.1016/s0021-9258(18)92736-5
发表时间:
1991-07
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
C. Hekman;J. Tomich;Y. Hatefi
通讯作者:
C. Hekman;J. Tomich;Y. Hatefi
DOI:
--
发表时间:
1991
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Bianchet,M;Ysern,X;Hullihen,J;Pedersen,PL;Amzel,LM
通讯作者:
Amzel,LM
影响因子:
2.1
作者:
DiezGonzalez, F;Russell, JB
通讯作者:
Russell, JB
影响因子:
2.9
作者:
Mendel-Hartvig,J;Capaldi,RA
通讯作者:
Capaldi,RA
影响因子:
2.9
作者:
Lücken,U;Gogol,EP;Capaldi,RA
通讯作者:
Capaldi,RA