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. 1990 Aug;93(4):1376–1382. doi: 10.1104/pp.93.4.1376

A Kinetic Characterization of Slow Inactivation of Ribulosebisphosphate Carboxylase during Catalysis

Daryl L Edmondson 1,1, Murray R Badger 1, T John Andrews 1
PMCID: PMC1062683  PMID: 16667628

Abstract

The catalytic activity of ribulosebisphosphate carboxylase (Rubisco) declined as soon as catalysis was initiated by exposure to its substrate, d-ribulose-1,5-bisphosphate (ribulose-P2). The decline continued exponentially, with a half-time of approximately 7 minutes until, eventually, a steady state level of activity was reached which could be as low as 15% of the initial activity. The ratio of the steady state activity to the initial activity was lower at low CO2 concentration and at low pH. The inhibitors 6-phosphogluconate and H2O2 alleviated the inactivation, increasing the final/initial rate ratio and the half-time. Varying ribulose-P2 concentration in the range above that required to saturate catalysis did not affect the kinetics of inactivation. The affinities for CO2 and ribulose-P2 were unaffected by the inactivation. The decline in activity occurred with preparations of ribulose-P2 which contained no detectable d-xylulose-1,5-bisphosphate and also with ribulose-P2 which had been generated enzymatically immediately before use. Inclusion of an aldolase system for removing d-xylulose-1,5-bisphosphate also did not alter the inactivation process. The inactivated Rubisco did not recover after complete exhaustion of ribulose-P2. We conclude that the inactivation is not caused by readily-reversible binding of ribulose-P2 at a site different from the active site and that it is unlikely to be attributable to inhibitory contaminants in ribulose-P2 preparations.

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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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