Regulation of proton flow and ATP synthesis in chloroplasts.
The chloroplast ATP synthase is strictly regulated so that it is very active in the light (rates of ATP synthesis can be higher than 5 micromol/min/mg protein), but virtually inactive in the dark. The subunits of the catalytic portion of the ATP synthase involved in activation, as well as the effects of nucleotides are discussed. The relation of activation to proton flux through the ATP synthase and to changes in the structure of enzyme induced by the proton electrochemical gradient are also presented. It is concluded that the gamma and epsilon subunits of CF(1) play key roles in both regulation of activity and proton translocation.
Evron
Y
Y
Department of Biology, Johns Hopkins University, 3400 N. Charles Street, Baltimore, Maryland 21218, USA.
Johnson
E A
EA
McCarty
R E
RE
D000255:Adenosine Triphosphate / Q000096:biosynthesis*; D025222:Chloroplast Proton-Translocating ATPases / Q000737:chemistry / Q000378:metabolism*; D002736:Chloroplasts / Q000378:metabolism*; D008954:Models, Biological; D008958:Models, Molecular; D009711:Nucleotides / Q000494:pharmacology; D021122:Protein Subunits; D018892:Proton-Motive Force
D009711:Nucleotides; D021122:Protein Subunits; D000255:Adenosine Triphosphate; D025222:Chloroplast Proton-Translocating ATPases