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Article

Aqueous access pathways in subunit a of rotary ATP synthase extend to both sides of the membrane.

Proceedings of the National Academy of Sciences of the United States of America - 11 Nov 2003

Angevine Christine M, Herold Kelly A G, Fillingame Robert H

Abstract excerpt

The role of subunit a in promoting proton translocation and rotary motion in the Escherichia coli F1Fo ATP synthase is poorly understood. In the membrane-bound Fo sector of the enzyme, H+ binding and release occur at Asp-61 in the middle of the second transmembrane helix (TMH) of subunit c. Proto...

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PMID: 14595019
DOI: 10.1073/pnas.2234364100
PMCID: PMC263739

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-14595019-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

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