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 Lettjournal_title
FEBS lettersauthors
Kaim G,Prummer M,Sick B,Zumofen G,Renn A,Wild UP,Dimroth Pdoi
10.1016/s0014-5793(02)03097-1keywords:
subject
Has Abstractpub_date
2002-08-14 00:00:00pages
156-63issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579302030971journal_volume
525pub_type
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