Revisão Acesso aberto Revisado por pares

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

2000; Elsevier BV; Volume: 1458; Issue: 2-3 Linguagem: Inglês

10.1016/s0005-2728(00)00082-7

ISSN

1879-2650

Autores

Joachim Weber, Alan E. Senior,

Tópico(s)

Biochemical and Molecular Research

Resumo

In ATP synthase, X-ray structures, demonstration of ATP-driven gamma-subunit rotation, and tryptophan fluorescence techniques to determine catalytic site occupancy and nucleotide binding affinities have resulted in pronounced progress in understanding ATP hydrolysis, for which a mechanism is presented here. In contrast, ATP synthesis remains enigmatic. The molecular mechanism 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. Techniques 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.

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