ATP synthase: what we know about ATP hydrolysis and what we do not know about ATP synthesis

Citation
J. Weber et Ae. Senior, ATP synthase: what we know about ATP hydrolysis and what we do not know about ATP synthesis, BBA-BIOENER, 1458(2-3), 2000, pp. 300-309
Citations number
44
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
ISSN journal
00052728 → ACNP
Volume
1458
Issue
2-3
Year of publication
2000
Pages
300 - 309
Database
ISI
SICI code
0005-2728(20000531)1458:2-3<300:ASWWKA>2.0.ZU;2-Q
Abstract
In ATP synthase. X-ray structures, demonstration of ATP-driven gamma-subuni t rotation, and tryptophan fluorescence techniques to determine catalytic s ite occupancy and nucleotide binding affinities have resulted in pronounced progress in understanding ATP hydrolysis, for which a mechanism is present ed here. In contrast, ATP synthesis remains enigmatic. The molecular mechan ism by which ADP is bound in presence of a high ATP/ADP concentration ratio is a fundamental unknown: similarly P-i binding is not understood. Techniq ues to measure catalytic site occupancy and ligand binding affinity changes during net ATP synthesis are much needed. Relation of these parameters to gamma-rotation is a further goal. A speculative model for ATP synthesis is offered. (C) 2000 Elsevier Science B.V. All rights reserved.