期刊
BIOPHYSICAL JOURNAL
卷 86, 期 3, 页码 1332-1344出版社
CELL PRESS
DOI: 10.1016/S0006-3495(04)74205-8
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资金
- NCRR NIH HHS [P41 RR005969, 5 P41 RR05969] Funding Source: Medline
- NIGMS NIH HHS [GM-23105, R01 GM023105, R01 GM067887, 1 R01 GM067887, R37 GM023105] Funding Source: Medline
F1F0-ATP synthase is a ubiquitous membrane protein complex that efficiently converts a cell's transmembrane proton gradient into chemical energy stored as ATP. The protein is made of two molecular motors, F-0 and F-1, which are coupled by a central stalk. The membrane unit, F-0, converts the transmembrane electrochemical potential into mechanical rotation of a rotor in F-0 and the physically connected central stalk. Based on available data of individual components, we have built an all-atom model of F-0 and investigated through molecular dynamics simulations and mathematical modeling the mechanism of torque generation in F-0. The mechanism that emerged generates the torque at the interface of the a- and c-subunits of F-0 through side groups aSer-206, aArg-210, and aAsn-214 of the a-subunit and side groups cAsp-61 of the c-subunits. The mechanism couples protonation/deprotonation of two cAsp-61 side groups, juxtaposed to the a-subunit at any moment in time, to rotations of individual c-subunit helices as well as rotation of the entire c-subunit. The aArg-210 side group orients the cAsp-61 side groups and, thereby, establishes proton transfer via aSer-206 and aAsn-214 to proton half-channels, while preventing direct proton transfer between the half-channels. A mathematical model proves the feasibility of torque generation by the stated mechanism against loads typical during ATP synthesis; the essential model characteristics, e.g., helix and subunit rotation and associated friction constants, have been tested and furnished by steered molecular dynamics simulations.
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