The rotary mechanism of ATP synthase.

TitleThe rotary mechanism of ATP synthase.
Publication TypeJournal Article
Year of Publication2000
AuthorsStock, D, Gibbons, C, Arechaga, I, Leslie, AG, Walker, JE
JournalCurr Opin Struct Biol
Volume10
Issue6
Pagination672-9
Date Published2000 Dec
ISSN0959-440X
KeywordsModels, Molecular, Protein Conformation, Proton-Translocating ATPases
Abstract

Since the chemiosmotic theory was proposed by Peter Mitchell in the 1960s, a major objective has been to elucidate the mechanism of coupling of the transmembrane proton motive force, created by respiration or photosynthesis, to the synthesis of ATP from ADP and inorganic phosphate. Recently, significant progress has been made towards establishing the complete structure of ATP synthase and revealing its mechanism. The X-ray structure of the F(1) catalytic domain has been completed and an electron density map of the F(1)-c(10) subcomplex has provided a glimpse of the motor in the membrane domain. Direct microscopic observation of rotation has been extended to F(1)-ATPase and F(1)F(o)-ATPase complexes.

DOI10.1016/s0959-440x(00)00147-0
Alternate JournalCurr. Opin. Struct. Biol.
Citation Key10.1016/s0959-440x(00)00147-0
PubMed ID11114504