Abstract
The carbon isotope effect at CO2 has been measured in the carboxylation of ribulose 1,5-bisphosphate by the ribulosebisphosphate carboxylase from Rhodospirillum rubrum. The isotope effect is obtained by comparing the isotopic composition of carbon 1 of the 3-phosphoglyceric acid formed in the reaction with that of the carbon dioxide source. A correction is made for carbon 1 of 3-phosphoglyceric acid which arises from carbon 3 of the starting ribulose bisphosphate. The isotope effect is k12/k13 = 1.0178 +/- 0.0008 at 25 degrees C, pH 7.8. This value is smaller than the corresponding value for the spinach enzyme. It appears that substrate addition with the R. rubrum enzyme is principally ordered, with ribulose bisphosphate binding first, whereas substrate addition is random with the spinach enzyme. The carboxylation step is partially rate limiting with both enzymes.
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