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. 1986 Dec;82(4):967–971. doi: 10.1104/pp.82.4.967

Activation of Ribulosebisphosphate Carboxylase/Oxygenase at Physiological CO2 and Ribulosebisphosphate Concentrations by Rubisco Activase

Archie R Portis Jr 1, Michael E Salvucci 1,1, William L Ogren 1
PMCID: PMC1056242  PMID: 16665175

Abstract

The enzyme-catalyzed activation of ribulosebisphosphate carboxylase/oxygenase (rubisco) was investigated in an illuminated reconstituted system containing thylakoid membranes, rubisco, ribulosebisphosphate (RuBP), MgCl2, carbonic anhydrase, catalase, the artificial electron acceptor pyocyanine, and partially purified rubisco activase. Optimal conditions for light-induced rubisco activation were found to include 100 micrograms per milliliter rubisco, 300 micrograms per milliliter rubisco activase, 3 millimolar RuBP, and 6 millimolar free Mg2+ at pH 8.2. The half-time for rubisco activation was 2 minutes, and was 4 minutes for rubisco deactivation. The rate of rubisco deactivation was identical in the presence and absence of activase. The Kact(CO2) of rubisco activation in the reconstituted system was 4 micromolar CO2, compared to a Kact(CO2) of 25 to 30 micromolar CO2 for the previously reported spontaneous CO2/Mg2+ activation mechanism. The activation process characterized here explains the high degree of rubisco activation at the physiological concentrations of 10 micromolar CO2 and 2 to 4 millimolar RuBP found in intact leaves, conditions which lead to almost complete deactivation of rubisco in vitro.

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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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