Wheat ribulose bisphosphate carboxylase can be converted from the slowly activating into the rapidly activating form by heat or effectors in the absence of CO2 and Mg2+. This conversion process had the same energy of activation of 95.6kJ/mol both in the presence and in the absence of effectors, whereas the free-energy change value ranged from +2.5kJ/mol to −3.4kJ/mol depending on the end product involved. Far-u.v. c.d. spectra measured before and after conversion indicated that ribulose bisphosphate carboxylase is an alpha/beta-class protein and that no significant changes in gross conformation occur. Signals in the near-u.v. region suggested that the main change during conversion is re-orientation of aromatic side chains, probably near the active site; a possible site for effector binding is discussed.
An upper limit to the active site concentration of ribulose bisphosphate carboxylase in chloroplasts
