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Article

Molecular mechanism of the ATP synthase's F(o) motor probed by mutational analyses of subunit a.

Journal of molecular biology - 13 Sept 2002

Wehrle Franziska, Kaim Georg, Dimroth Peter

Abstract excerpt

The most prominent residue of subunit a of the F(1)F(o) ATP synthase is a universally conserved arginine (aR227 in Propionigenium modestum), which was reported to permit no substitution with retention of ATP synthesis or H(+)-coupled ATP hydrolysis activity. We show here that ATP synthases with R227K or R227H mutations in the P.modestum a subunit catalyse ATP-driven Na(+) transport above or below pH 8.0,...

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Source

Identifiers

PMID: 12217697
DOI: 10.1016/s0022-2836(02)00731-3

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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