The mechanism of Rubisco-catalysed oxygenation.
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the cornerstone of photosynthetic carbon assimilation because it catalyses the fixation of CO2 onto ribulose-1,5-bisphosphate (RuBP). The enzyme also catalyses RuBP oxygenation, thereby evolving phosphoglycolate which is recycled along the photorespiratory pathway. Oxygenation is quantitatively important, because under ordinary gaseous conditions, more than one third of RuBP molecules are oxygenated rather than carboxylated. However, contrary to carboxylation, the chemical mechanism of oxygenation is not well known, and little progress has been made since the early 80s. Here, I review recent experimental data that provide some new insights into the reaction mechanism, and carry out simple calculations of kinetic parameters. Isotope effects suggest that oxygenation is less likely initiated by a redox phenomenon (such as superoxide production) and more likely involves concerted chemical events that imply interactions with protons. A possible energy profile of the reaction is drawn which suggests that the generation of the oxygenated reaction intermediate (peroxide) is irreversible. Possible changes in oxygenation-associated rate constants between Rubisco forms are discussed.
Research School of Biology, ANU College of Medicine, Biology and Environment, Australian National University, Canberra, 2601, ACT, Australia.
Guillaume
G
Tcherkez
D055162:Biocatalysis; D007700:Kinetics; D010100:Oxygen / Q000378:metabolism*; D010103:Oxygen Isotopes; D012273:Ribulose-Bisphosphate Carboxylase / Q000378:metabolism*; D013816:Thermodynamics
D010103:Oxygen Isotopes; D012273:Ribulose-Bisphosphate Carboxylase; D010100:Oxygen
CO2; carbon reactions; carboxylation; nutrients/nitrogen; photosynthesis