[Allosteric properties of CF1-ATPase form chloroplasts].
The inhibiting effect of ADP and Mg2+ on CF1-ATPase from chloroplasts depending on their concentration, pH and the presence of stimulating agents of various origin was studied. It was shown that the low Mg-dependent activity of the soluble enzyme is due to non-competitive inhibition of the reaction by Mg2+ in the presence of ADP. The CF1-ATPase stimulators lower the inhibiting effect, thus allowing to detect the "true" Mg-dependent activity of the enzyme. The data obtained are indicative of the existence of Mg2+- and ADP-specific sitein the enzyme, which controls its catalytic activity. The properties and possible role of this site in photophosphorylation are discussed.
D000244:Adenosine Diphosphate / Q000494:pharmacology; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000494:Allosteric Regulation; D000495:Allosteric Site; D002736:Chloroplasts / Q000201:enzymology*; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D010944:Plants / Q000201:enzymology; D006180:Proton-Translocating ATPases
D000244:Adenosine Diphosphate; D000251:Adenosine Triphosphatases; D006180:Proton-Translocating ATPases; D008274:Magnesium
Allostericheskie svoistva CF1-ATPazy khloroplastov.