Coupled rotation within single F0F1 enzyme complexes during ATP synthesis or hydrolysis.

Abstract:

:F0F1 ATP synthases are the smallest rotary motors in nature and work as ATP factories in bacteria, plants and animals. Here we report on the first observation of intersubunit rotation in fully coupled single F0F1 molecules during ATP synthesis or hydrolysis. We investigate the Na+-translocating ATP synthase of Propionigenium modestum specifically labeled by a single fluorophore at one c subunit using polarization-resolved confocal microscopy. Rotation during ATP synthesis was observed with the immobilized enzyme reconstituted into proteoliposomes after applying a diffusion potential, but not with a Na+ concentration gradient alone. During ATP hydrolysis, stepwise rotation of the labeled c subunit was found in the presence of 2 mM NaCl, but not without the addition of Na+ ions. Moreover, upon the incubation with the F0-specific inhibitor dicyclohexylcarbodiimide the rotation was severely inhibited.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Kaim G,Prummer M,Sick B,Zumofen G,Renn A,Wild UP,Dimroth P

doi

10.1016/s0014-5793(02)03097-1

keywords:

subject

Has Abstract

pub_date

2002-08-14 00:00:00

pages

156-63

issue

1-3

eissn

0014-5793

issn

1873-3468

pii

S0014579302030971

journal_volume

525

pub_type

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