Department of Environmental Biology, Research School of Biological Sciences, The Australian National University, Canberra, Australia
Abstract:
Ribulose-1,5-bisphosphate oxygenase was activated by incubation with CO2 and Mg2+ and inactivated upon removal of CO2 and Mg2+ by gel filtration. The activity of the enzyme was dependent upon the preincubation concentrations of CO2 and Mg2+ and upon the preincubation pH. This indicated that activation involved the reversible formation of an equilibrium complex of enzyme-CO2-Mg. The kinetics of the activation process were the same as those described by G. H. Lorimer et al. ((1976) Biochemistry15, 529–536), for ribulose bisphosphate carboxylase and are consistent with the ordered reversible reaction sequence:
