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Trends Biochem Sci. 1994 Jul;19(7):284-9.

Coupling between catalytic sites and the proton channel in F1F0-type ATPases.

Author information

1
Institute of Molecular Biology, University of Oregon, Eugene 97403.

Abstract

F1F0-type ATPases catalyse both ATP-driven proton translocation and proton-gradient-driven ATP synthesis. Recent cryoelectronmicroscopy and low-resolution X-ray studies provide a first glimpse at the structure of this complicated membrane-bound enzyme. The F1 part is roughly globular and linked to the membrane-intercalated F0 part by a narrow stalk domain, which contains the gamma-, delta- and epsilon-subunits along with domains of the b-subunit of the F0 part. Here, we review evidence that conformational and positional changes in the gamma- and epsilon-subunits provide the coupling between catalytic sites and proton translocation within the F1F0 complex.

PMID:
8048168
DOI:
10.1016/0968-0004(94)90006-x
[Indexed for MEDLINE]

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