Rubisco, formally known as ribulose‐1,5‐bisphosphate (RuBP) carboxylase/oxygenase, is the chloroplast enzyme that assimilates atmospheric carbon dioxide during photosynthesis by combining it with RuBP to form two molecules of phosphoglycerate. However, Rubisco allows oxygen to react with RuBP in addition to carbon dioxide, producing phosphoglycolate, and thereby also initiates the process known as photorespiration. Genetic modification to overcome the limitations of Rubisco would have great agronomic importance.

Keywords: photosynthesis; photorespiration; chloroplast

Figure 1.

Structures of a higher plant (a) and a prokaryotic (b) Rubisco (Protein Data Bank entries 8RUC and 9RUB, respectively). Small subunits in the higher plant form are coloured blue and green. RuBP, located at the active site, is visible (coloured blue) in the prokaryotic structure depicted, but the active site is not visible in this higher plant structure.

Figure 2.

Synthesis of Rubisco. Adapted from Rodermel SR, Haley J, Jiang CZ, Tsai CH and Bogorad L (1996) A mechanism for intergenomic integration – abundance of ribulose bisphosphate carboxylase small‐subunit protein influences the translation of the large‐subunit mRNA. Proceedings of the National Academy of Sciences of the USA 93: 3881–3885.

Figure 3.

Catalytic cycle of carboxylation and oxygenation by Rubisco. Adapted from Hartmen FC and Harpel MR (1994) Structure, function, regulation, and assembly of D‐ribulose‐1,5‐bisphosphate carboxylase/oxygenase. Annual Review of Biochemistry 63: 197–234.

Figure 4.

Principles of regulation of Rubisco catalytic activity. [E], decarbamylated Rubisco; [E.I], decarbamylated enzyme with substrate (ribulose 1,5‐bisphosphate, RuBP) or misfire product (xylulose 1,5‐bisphosphate, XuBP) bound at active sites – in this context both compounds are inhibitors (I); [E.CO2.Mg2+], ternary complex with catalytically competent active site geometry; [E.CO2.Mg2+.I], carbamylated enzyme with catalytic site occupied by tight binding inhibitor (e.g. carboxyarabinitol 1‐phosphate (CA1P), pentodiulose 1,5‐bisphosphate (PDBP) and possibly 3‐ketoarabinitol 1,5‐bisphosphate (KABP)). Redrawn from Parry et al. , with permission from the Society for Experimental Biology.



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Further Reading

Andersson I (1996) Large structures at high resolution: the 1.6 angstrom crystal structure of spinach ribulose‐1,5‐bisphosphate carboxylase/oxygenase complexed with 2‐carboxyarabinitol bisphosphate. Journal of Molecular Biology 259: 160–174.

Gatenby AA and Ellis RJ (1990) Chaperone function: the assembly of ribulose bisphosphate carboxylase‐oxygenase. Annual Review of Cell Biology 6: 125–149.

Portis AR Jr (1992) Regulation of ribulose 1,5‐bisphosphate carboxylase/oxygenase activity. Annual Review of Plant Physiology and Plant Molecular Biology 43: 415–437.

Portis AR Jr, Li C, Wang D and Salvucci ME (2008) Regulation of Rubisco activase and its interaction with Rubisco. Journal of Experimental Botany 59: 1597–1604.

Portis AR Jr and Parry MAJ (2007) Discoveries in Rubisco (ribulose 1,5‐bisphosphate carboxylase/oxygenase): a historical perspective. Photosynthesis Research 94: 121–143.

Sage RF, Way DA and Kubien DS (2008) Rubisco, Rubisco activase, and global climate change. Journal of Experimental Botany 59: 1581–1595.

Spreitzer RJ and Salvucci ME (2002) RUBISCO: Structure, regulatory interactions, and possibilities for a better enzyme. Annual Review of Plant Physiology and Plant Molecular Biology 53: 449–475.

Tabita FR, Satagopan S, Hanson TE, Kreel NE and Scott SS (2008) Distinct form I, II, III, and IV Rubisco proteins from the three kingdoms of life provide clues about Rubisco evolution and structure/function relationships. Journal of Experimental Botany 59: 1515–1524.

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Portis, Archie R, and Parry, Martin AJ(Mar 2009) Rubisco. In: eLS. John Wiley & Sons Ltd, Chichester. [doi: 10.1002/9780470015902.a0001293.pub2]