The rotary mechanism sf ATP synthase

Citation
D. Stock et al., The rotary mechanism sf ATP synthase, CURR OP STR, 10(6), 2000, pp. 672-679
Citations number
63
Categorie Soggetti
Biochemistry & Biophysics
Journal title
CURRENT OPINION IN STRUCTURAL BIOLOGY
ISSN journal
0959440X → ACNP
Volume
10
Issue
6
Year of publication
2000
Pages
672 - 679
Database
ISI
SICI code
0959-440X(200012)10:6<672:TRMSAS>2.0.ZU;2-7
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 tr ansmembrane proton motive force, created by respiration or photosynthesis, to the synthesis of ATP from ADP and inorganic phosphate. Recently, signifi cant progress has been made towards establishing the complete structure of ATP synthase and revealing its mechanism. The X-ray structure of the F-1 ca talytic 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 F1Fo-ATPase complexes.