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JXB Advance Access originally published online on April 15, 2008
Journal of Experimental Botany 2008 59(7):1555-1568; doi:10.1093/jxb/ern091
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© The Author [2008]. Published by Oxford University Press [on behalf of the Society for Experimental Biology]. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

SPECIAL ISSUE REVIEW PAPER

Catalysis and regulation in Rubisco

Inger Andersson*

Department of Molecular Biology, Swedish University of Agricultural Sciences, BMC Box 590, S-751 24 Uppsala, Sweden

* E-mail: inger{at}xray.bmc.uu.se

Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyses the incorporation of inorganic CO2 into the organic molecules of life. Rubisco is extremely inefficient as a catalyst and its carboxylase activity is compromised by numerous side-reactions including oxygenation of its sugar phosphate substrate by atmospheric O2. The reduction in the catalytic efficiency as a result of these processes has implications for crop yield, nitrogen and water usage, and for the global carbon cycle. Several aspects of Rubisco including its complex biosynthesis and multi-step catalytic reaction are subject to tight control involving light, cellular metabolites, and molecular chaperones. Numerous high-resolution crystal structures of different forms of Rubisco are now available, including structures of mutant enzymes. These provide a molecular framework for the understanding of these processes at the molecular level.

Key words: Carbon fixation, CO2/O2 specificity, light-regulation, Rubisco, structure–function studies

Abbreviations: Rubisco, ribulose-1,5-bisphosphate carboxylase/oxygenase; RuBP, D-ribulose-1,5-bisphosphate; 3PGA, 3-phospho-D-glycerate; RLP, Rubisco-like protein; L, large subunit; S, small subunit; rbcL, Rubisco large subunit gene; rbcS, Rubisco small subunit gene; 2CABP, 2'-carboxyarabinitol-1,5-bisphosphate; CA1P, 2'-carboxyarabinitol-1-phosphate; XuBP, D-xylulose-1,5-bisphosphate.

Received 6 February 2008; Revised 5 March 2008 Accepted 6 March 2008


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