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.
| Original language | English |
|---|---|
| Pages (from-to) | 1555-1568 |
| Number of pages | 14 |
| Journal | Journal of Experimental Botany |
| Volume | 59 |
| Issue number | 8 |
| DOIs | |
| Publication status | Published - 2008 |
Keywords
- carbon fixation
- CO(2)/O(2) specificity
- light-regulation
- Rubisco
- structure-function studies
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