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| Mechanism of the F1F0-type ATP synthase, a biological rotary motor |
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| Author(s): Capaldi RA, Aggeler R |
| Source: TRENDS IN BIOCHEMICAL SCIENCES Volume: 27 Issue: 3 Pages: 154-160 Published: MAR 2002 |
| Times Cited: 158 References: 49 |
| Abstract: The F1F0-type ATP synthase is a key enzyme in cellular energy interconversion. During ATP synthesis, this large protein complex uses a proton gradient and the associated membrane potential to synthesize ATP It can also reverse and hydrolyze ATP to generate a proton gradient. The structure of this enzyme in different functional forms is now being rapidly elucidated. The emerging consensus is that the enzyme is constructed as two rotary motors, one in the F-1 part that links catalytic site events with movements of an internal rotor, and the other in the F-0 part, linking proton translocation to movements of this F-0 rotor. Although both motors can work separately, they must be connected together to interconvert energy. Evidence for the function of the rotary motor, from structural, genetic and biophysical studies, is reviewed here, and some uncertainties and remaining mysteries of the enzyme mechanism are also discussed. |
| Document Type: Review |
| Language: English |
| Reprint Address: Capaldi, RA (reprint author), Univ Oregon, Inst Mol Biol, Eugene, OR 97403 USA |
Addresses:
1. Univ Oregon, Inst Mol Biol, Eugene, OR 97403 USA |
| Publisher: ELSEVIER SCIENCE LONDON, 84 THEOBALDS RD, LONDON WC1X 8RR, ENGLAND |
| Subject Category: Biochemistry & Molecular Biology |
| IDS Number: 531LK |
| ISSN: 0968-0004 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |