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Article

ATP synthase with its gamma subunit reduced to the N-terminal helix can still catalyze ATP synthesis.

The Journal of biological chemistry - 25 Sept 2009

Mnatsakanyan Nelli, Hook Jonathon A, Quisenberry Leah, Weber Joachim

Abstract excerpt

ATP synthase uses a unique rotary mechanism to couple ATP synthesis and hydrolysis to transmembrane proton translocation. As part of the synthesis mechanism, the torque of the rotor has to be converted into conformational rearrangements of the catalytic binding sites on the stator to allow synthesis and release of ATP. The gamma subunit of the rotor, which plays a central role in the energy conversion, consists...

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Identifiers

PMID: 19636076
DOI: 10.1074/jbc.M109.030528
PMCID: PMC2785340

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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