ATP synthase: an electrochemical transducer with rotatory mechanics

Autor(en): Junge, W 
Lill, H
Engelbrecht, S
Stichwörter: ADENOSINE-TRIPHOSPHATASE; ATPASES; BINDING; Biochemistry & Molecular Biology; CHLOROPLAST; EPSILON-SUBUNIT; ESCHERICHIA-COLI F1-ATPASE; F1F0; H+/ATP COUPLING RATIO; PROTON CHANNEL; RECONSTITUTION
Erscheinungsdatum: 1997
Herausgeber: ELSEVIER SCI LTD
Journal: TRENDS IN BIOCHEMICAL SCIENCES
Volumen: 22
Ausgabe: 11
Startseite: 420
Seitenende: 423
Zusammenfassung: 
ATP synthase (F0F1-ATPase) uses proton-or sodium-motive force to produce ATP from ADP and P-i. Three lines of experiment have recently demonstrated large-scale intersubunit rotation during ATP hydrolysis by F-1. We discuss how ion flow through the membrane-intrinsic portion, F-0, may generate torque and how this might be transmitted between stator and rotor to finally expel spontaneously formed ATP from F-1 into water.
ISSN: 09680004
DOI: 10.1016/S0968-0004(97)01129-8

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