Andersson, Inger
- Department of Molecular Biology, Swedish University of Agricultural Sciences
Abstract
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyses the incorporation of inorganic CO(2) 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 O(2). 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.
Keywords
carbon fixation; CO(2)/O(2) specificity; light-regulation; Rubisco; structure-function studies
Published in
Journal of Experimental Botany
2008, volume: 59, number: 8, pages: 1555-1568
Publisher: Oxford Journals
SLU Authors
UKÄ Subject classification
Environmental Sciences and Nature Conservation
Forest Science
Publication identifier
- DOI: https://doi.org/10.1093/jxb/ern091
Permanent link to this page (URI)
https://res.slu.se/id/publ/31350