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Regulation of bacterial ATP synthase activity: A gear‐shifting or a pawl–ratchet mechanism?
Author(s) -
MirandaAstudillo Héctor,
ZarcoZavala Mariel,
GarcíaTrejo José J.,
GonzálezHalphen Diego
Publication year - 2021
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.15671
Subject(s) - atp synthase , atp synthase gamma subunit , atp hydrolysis , ratchet , v atpase , protein subunit , f atpase , atpase , chemiosmosis , microbiology and biotechnology , enzyme , biology , biophysics , chemistry , biochemistry , physics , work (physics) , gene , thylakoid , chloroplast , thermodynamics
The F 1 F o -ATP synthase, a widely distributed nanomotor responsible of ATP synthesis, rotates its central rotor reversibly: In the clockwise direction when viewed from the Fo (with the observer facing the positive side of the energy transducing membrane and looking down into the negative side of the membrane), it functions as ATP synthase, while in counterclockwise sense, it operates as a proton-pumping ATP hydrolase. Regulation exerted by naturally occurring inhibitory proteins of the enzyme appears to function by avoiding ATP hydrolysis while preserving ATP synthesis. The work of Liu et al. describes an unbiased, elegant analytical pipeline that provides important insights into the inhibitory role of the ε-subunit of the bacterial F 1 F o -ATP synthase in vivo. We discuss if a gear-shifting versus a pawl-ratchet mechanism may explain the regulatory role of the ε-subunit.