1995•University of North Texas Digital Library (University of North Texas)Open access

The nature and alternate rates of the ribulose 1,5-bisphosphate (RuBP) carboxylase/oxygenase (Rubisco) oxygenation intermediate

Mark R. Harpel, Yuh-Ru Chen, F.C. Hartman

Abstract

Mutant ribulose 1,5-bisphosphate (RuBP) were employed to investigate the partitioning of carbon flow between photosynthesis or photorespiration. Previous functional and structural studies implicate active site Lys329 and Glu48 or R. rubrum RuBp in promoting addition of CO2 to the RuBP-enediol. Two novel O2-dependent side products generated by the K329A and E49Q mutants provided insight into RuBP oxygenase intermediate and roles of Lys329 and Glu48 in oxygenation.

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Key concepts: Photorespiration, RuBisCO, Oxygenase, Ribulose 1,5-bisphosphate, Photosynthesis, Pyruvate carboxylase, Ribulose, Biochemistry