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FEBS Lett. 2003 Nov 27;555(1):29-34.

Mechanics of coupling proton movements to c-ring rotation in ATP synthase.

Author information

1
Department of Biomolecular Chemistry, 1300 University Avenue, University of Wisconsin Medical School, Madison, WI 53706, USA. rhfillin@facstaff.wisc.edu

Abstract

F1F0 ATP synthases generate ATP by a rotary catalytic mechanism in which H+ transport is coupled to rotation of an oligomeric ring of c subunits extending through the membrane. Protons bind to and then are released from the aspartyl-61 residue of subunit c at the center of the membrane. Subunit a of the F0 sector is thought to provide proton access channels to and from aspartyl-61. Here, we summarize new information on the structural organization of Escherichia coli subunit a and the mapping of aqueous-accessible residues in the second, fourth and fifth transmembrane helices (TMHs). Aqueous-accessible regions of these helices extend to both the cytoplasmic and periplasmic surface. We propose that aTMH4 rotates to alternately expose the periplasmic or cytoplasmic half-channels to aspartyl-61 of subunit c during the proton transport cycle. The concerted rotation of interacting helices in subunit a and subunit c is proposed to be the mechanical force driving rotation of the c-rotor, using a mechanism akin to meshed gears.

PMID:
14630314
DOI:
10.1016/s0014-5793(03)01101-3
[Indexed for MEDLINE]
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