In:
Science, American Association for the Advancement of Science (AAAS), Vol. 286, No. 5445 ( 1999-11-26), p. 1722-1724
Abstract:
F 0 F 1 , found in mitochondria or bacterial membranes, synthesizes adenosine 5′-triphosphate (ATP) coupling with an electrochemical proton gradient and also reversibly hydrolyzes ATP to form the gradient. An actin filament connected to a c subunit oligomer of F 0 was able to rotate by using the energy of ATP hydrolysis. The rotary torque produced by the c subunit oligomer reached about 40 piconewton-nanometers, which is similar to that generated by the γ subunit in the F 1 motor. These results suggest that the γ and c subunits rotate together during ATP hydrolysis and synthesis. Thus, coupled rotation may be essential for energy coupling between proton transport through F 0 and ATP hydrolysis or synthesis in F 1 .
Type of Medium:
Online Resource
ISSN:
0036-8075
,
1095-9203
DOI:
10.1126/science.286.5445.1722
Language:
English
Publisher:
American Association for the Advancement of Science (AAAS)
Publication Date:
1999
detail.hit.zdb_id:
128410-1
detail.hit.zdb_id:
2066996-3
detail.hit.zdb_id:
2060783-0
SSG:
11
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