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. 1978 Apr;61(4):680–687. doi: 10.1104/pp.61.4.680

Carbon Isotope Fractionation by Ribulose-1,5-Bisophosphate Carboxylase from Various Organisms 1

Marilyn F Estep 1, F Robert Tabita 1,2, Patrick L Parker 1, Chase Van Baalen 1
PMCID: PMC1091944  PMID: 16660363

Abstract

Carbon isotope fractionation by structurally and catalytically distinct ribulose-1,5-bisphosphate carboxylases from one eucaryotic and four procaryotic organisms has been measured under nitrogen. The average fractionation for 40 experiments was −34.1 ‰ with respect to the δ13C of the dissolved CO2 used, although average fractionations for each enzyme varied slightly: spinach carboxylase, −36.5 ‰; Hydrogenomonas eutropha, −38.7 ‰; Agmenellum quadruplicatum, −32.2 ‰; Rhodospirillum rubrum, −32.1 ‰; Rhodopseudomonas sphaeroides peak I carboxylase, −31.4 ‰; and R. sphaeroides peak II carboxylase, −28.3 ‰. The carbon isotope fractionation value was largely independent of method of enzyme preparation, purity, or reaction temperature, but in the case of spinach ribulose-1,5-bisphosphate carboxylase fractionation, changing the metal cofactor used for enzyme activation had a distinct effect on the fractionation value. The fractionation value of −36.5 ‰ with Mg2+ as activator shifted to −29.9 ‰ with Ni2+ as activator and to −41.7 ‰ with Mn2+ as activator. These dramatic metal effects on carbon isotope fractionation may be useful in examining the catalytic site of the enzyme.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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