Ribulose-1,5-bisphosphate carboxylase oxygenase, better known as RuBisCO,[note 1] is an enzyme that catalyzes the first major step of carbon fixation in the Calvin cycle. Carbon fixation is a process by which the atoms of atmospheric carbon dioxide are made available to organisms in the form of energy-rich molecules such as glucose. RuBisCO splits 6-C molecules into two equal parts.
RuBisCO is also the most abundant protein in leaves and the most abundant protein on Earth. It accounts for 50% of soluble leaf protein (20-30% of total leaf nitrogen) and 30% of soluble leaf protein in plants (5-9% of total leaf nitrogen).
Notes and references[change | change source]
- Wildman SG (2002). "Along the trail from fraction I protein to Rubisco (ribulose bisphosphate carboxylase-oxygenase)". Photosyn. Res. 73 (1-3): 243–50. . .
- Portis AR, Parry MA (October 2007). "Discoveries in Rubisco (Ribulose 1,5-bisphosphate carboxylase/oxygenase): a historical perspective". Photosyn. Res. 94 (1): 121–43. . .
- Cooper, Geoffrey M. (2000). "10.The Chloroplast Genome". The Cell: a molecular approach (2nd ed.). Washington, D.C: ASM Press. . http://www.ncbi.nlm.nih.gov/books/bv.fcgi?highlight=RuBisCO&rid=cooper.section.1655#1659. "One of the subunits of ribulose bisphosphate carboxylase (rubisco) is encoded by chloroplast DNA. Rubisco is the critical enzyme which catalyzes the addition of CO2 to ribulose-1,5-bisphosphate during the Calvin cycle (see Figure 2.39). Not only is it the major protein component of the chloroplast stroma but it is also thought to be the single most abundant protein on Earth, so it is noteworthy that one of its subunits is encoded by the chloroplast genome."
- Dhingra A, Portis AR, Daniell H (April 2004). "Enhanced translation of a chloroplast-expressed RbcS gene restores small subunit levels and photosynthesis in nuclear RbcS antisense plants". Proc. Natl. Acad. Sci. U.S.A. 101 (16): 6315–20. . . . "(Rubisco) is the most prevalent enzyme on this planet, accounting for 30–50% of total soluble protein in the chloroplast.".
- Feller U, Anders I, Mae T (2008). "Rubiscolytics: fate of Rubisco after its enzymatic function in a cell is terminated". J. Exp. Bot. 59 (7): 1615–24. . .
- Ellis, R. John 2010. Biochemistry: tackling unintelligent design. Nature 463, 164-165 doi:10.1038/463164a