page_title: RuBisCO
section_title: References
hierarchical_section_title: RuBisCO / References
context_page_description: Ribulose-1,5-bisphosphate carboxylase/oxygenase, commonly known by the abbreviations Rubisco, rubisco, RuBPCase, or RuBPco, is an enzyme involved in the first major step of carbon fixation, a process by which the atmospheric carbon dioxide is converted by plants and other photosynthetic organisms to energy-rich molecules such as glucose. In chemical terms, it catalyzes the carboxylation of ribulose-1,5-bisphosphate. It is probably the most abundant enzyme on Earth.
context_section_description: Sharkey, TD (2018). "Discovery of the canonical Calvin-Benson cycle". Photosynth Res. 53: 835–18.
  Cooper, Geoffrey M. (2000). "10.The Chloroplast Genome". The Cell: A Molecular Approach (2nd ed.). Washington, D.C: ASM Press. ISBN 978-0-87893-106-4. , one of the subunits of ribulose bisphosphate carboxylase (rubisco) is encoded by chloroplast DNA. Rubisco is the critical enzyme that catalyzes the addition of CO
  2 to ribulose-1,5-bisphosphate during the Calvin cycle. 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". Proceedings of the National Academy of Sciences of the United States of America. 101 (16): 6315–20. Bibcode:2004PNAS..101.6315D. doi:10.1073/pnas.0400981101. PMC 395966. PMID 15067115. (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" (PDF). Journal of Experimental Botany. 59 (7): 1615–24. doi:10.1093/jxb/erm242. PMID 17975207.
  (Entrez GeneID: )
  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". Proceedings of the National Academy of Sciences of the United States of America. 101 (16): 6315–20. Bibcode:2004PNAS..101.6315D. doi:10.1073/pnas.0400981101. PMC 395966. PMID 15067115.
  Arabidopsis thaliana has four RuBisCO small chain genes.
  Yoon M, Putterill JJ, Ross GS, Laing WA (April 2001). "Determination of the relative expression levels of rubisco small subunit genes in Arabidopsis by rapid amplification of cDNA ends". Analytical Biochemistry. 291 (2): 237–44. doi:10.1006/abio.2001.5042. PMID 11401297.
  Stryer, Lubert; Berg, Jeremy Mark; Tymoczko, John L. (2002). "20. The Calvin Cycle and the Pentose Phosphate Pathway". Biochemistry (5th ed.). San Francisco: W.H. Freeman. ISBN 978-0-7167-3051-4. Figure 20.3.  Structure of Rubisco. (Color-coded ribbon diagram)
  The structure of RuBisCO from the photosynthetic bacterium  Rhodospirillum rubrum has been determined by X-ray crystallography, see: PDB: 9RUB​. A comparison of the structures of eukaryotic and bacterial RuBisCO is shown in the Protein Data Bank feature article on Rubisco.
  Molecular Cell Biology, 4th edition, by Harvey Lodish, Arnold Berk, S. Lawrence Zipursky, Paul Matsudaira, David Baltimore and James E. Darnell. Published by W. H. Freeman & Co. (2000) New York. Online textbook. Figure 16-48 shows a structural model of the active site, including the involvement of magnesium. The Protein Data Bank feature article on RuBisCO also includes a model of magnesium at the active site Archived 2006-01-09 at the Wayback Machine.
  Stec B (November 2012). "Structural mechanism of RuBisCO activation by carbamylation of the active site lysine". Proceedings of the National Academy of Sciences of the United States of America. 109 (46): 18785–90. Bibcode:2012PNAS..10918785S. doi:10.1073/pnas.1210754109. PMC 3503183. PMID 23112176.
  The Lodish textbook describes the localization of RuBisCO to the stromal space of chloroplasts. Figure 17-7 illustrates how RuBisCO small subunits move into the chloroplast stroma and assemble with the large subunits.
  Andersson, Inger (May 2008). "Catalysis and regulation in Rubisco". Journal of Experimental Botany. 59 (7): 1555–1568. doi:10.1093/jxb/ern091. PMID 18417482.
  Erb, Tobias; Zarzycki, Jan (February 2018). "A short history of RubisCO: the rise and fall (?) of Nature's predominant CO₂ fixing enzyme". Current Opinion in Biotechnology. 49: 100–107. doi:10.1016/j.copbio.2017.07.017. PMID 28843191.
  Schneider, Gunter; Lundqvis, Tomas (5 July 1991). "Crystal Structure of Activated Ribulose- 1,5-bisphosphate Carboxylase Complexed with Its 
caption: Figure 3. In this figure, each protein chain in the (LS)2 complex is given its own color for easy identification.
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