The chloroplast ATP synthase: A rotary enzyme?

Citation
Re. Mccarty et al., The chloroplast ATP synthase: A rotary enzyme?, ANN R PLANT, 51, 2000, pp. 83-109
Citations number
94
Categorie Soggetti
Plant Sciences","Animal & Plant Sciences
Journal title
ANNUAL REVIEW OF PLANT PHYSIOLOGY AND PLANT MOLECULAR BIOLOGY
ISSN journal
10402519 → ACNP
Volume
51
Year of publication
2000
Pages
83 - 109
Database
ISI
SICI code
1040-2519(2000)51:<83:TCASAR>2.0.ZU;2-#
Abstract
The chloroplast adenosine triphosphate (ATP) synthase is located in the thy lakoid membrane and synthesizes ATP from adenosine diphosphate and inorgani c phosphate at the expense of the electrochemical proton gradient formed by light-dependent electron flow. The structure, activities, and mechanism of the chloroplast ATP synthase are discussed. Emphasis is given to the inher ent structural asymmetry of the ATP synthase and to the implication of this asymmetry to the mechanism of ATP synthesis and hydrolysis. A critical eva luation of the evidence in support of and against the notion that one part of the enzyme rotates with respect to other parts during catalytic turnover is presented. It is concluded that although rotation can occur, whether it is required for activity of the ATP synthase has not been established uneq uivocally.