| Abstract: | A kinetic study of ATP hydrolysis by CF1-ATPase from chloroplasts in the presence of optimal concentrations of the stimulators, sodium sulfite and ethyl alcohol, has been carried out. At MgCl2/ATP ratios more than 1 the reaction kinetics obey the Michaelis--Menten equation. At ATP excess the kinetics are of the second order with respect to Mg2+. The data obtained are consistent with the hypothesis on the formation of an enzyme substrate Mg.CF1-MgATP complex containing beside Mg-ATP substrate Mg2+. The dependence of the maximal rate of the reaction on pH was studied. Two active groups with pK of 6.3 and 8.9 were revealed. The group responsible for Mg+2 binding to the enzyme has a pK of 8.3. The possible nature of the active groups of the enzyme is discussed. |
