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A reciprocating motion-driven rotation mechanism for the ATP synthase
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作者 Jiafeng Liu Xinmiao Fu Zengyi Chang 《Science China(Life Sciences)》 SCIE CAS CSCD 2016年第1期44-48,共5页
The ATP synthase (having a typical subunit composition of α3β3γeab2c8-15) employs an intriguing rotary mechanism for the generation of ATP from ADP and Pi, using energy stored in a transmembrane proton gradient. ... The ATP synthase (having a typical subunit composition of α3β3γeab2c8-15) employs an intriguing rotary mechanism for the generation of ATP from ADP and Pi, using energy stored in a transmembrane proton gradient. The conventional rotary model, although being generally accepted, remains difficult to explain certain experimental observations. Here we propose an alterna- tive rotary model for the ATP synthase such that what rotates is the catalytic α3β3 cylinder rather than the central stalk and the membrane-embedded c-ring. Specifically, the membrane translocation of protons would induce a cycled conformational change in the c-ring, leading to a reciprocating motion of the attached central stalk, which in turn drives the unidirectional rotation of the α3β3 cylinder. Such a reciprocating motion-driven rotation mechanism is somehow analogous to the working mechanism of a retractable click ballpoint pen. Our new model not only explains the experimental observations that have been difficult to reconcile with the conventional model but also avoids its theoretical illogicality. 展开更多
关键词 ATP synthase rotational catalysis rotary model
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