Discoveries in Rubisco (Ribulose 1,5-bisphosphate carboxylase/oxygenase): a historical perspective

@article{Portis2007DiscoveriesIR,
  title={Discoveries in Rubisco (Ribulose 1,5-bisphosphate carboxylase/oxygenase): a historical perspective},
  author={Archie R. Portis and Martin A. J. Parry},
  journal={Photosynthesis Research},
  year={2007},
  volume={94},
  pages={121-143}
}
  • A. Portis, M. Parry
  • Published 31 July 2007
  • Environmental Science
  • Photosynthesis Research
Historic discoveries and key observations related to Rubisco (Ribulose 1,5-bisphosphate carboxylase/oxygenase), from 1947 to 2006, are presented. Currently, around 200 papers describing Rubisco research are published each year and the literature contains more than 5000 manuscripts on the subject. While trying to ensure that all the major events over this period are recorded, this analysis will inevitably be incomplete and will reflect the areas of particular interest to the authors. 
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TLDR
The presented models serve as a theoretical framework to explain a wide range of observed kinetic properties of RuBisCOs derived from a variety of species and can support hypotheses about molecular mechanisms and can systematically compare enzymes from different origins.
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TLDR
The presented models serve as a theoretical framework to explain a wide range of observed kinetic properties of RuBisCOs derived from a variety of species and support hypotheses about molecular mechanisms and systematically compare enzymes from different origins.
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  • M. Hayer‐Hartl
  • Biology, Environmental Science
    Protein science : a publication of the Protein Society
  • 2017
TLDR
This review highlights the work toward understanding the structure and mechanism of these auxiliary machineries of Rubisco, which depend on an array of additional factors for assembly and metabolic repair.
Study of Ribulose 1, 5-Bisphosphate Carboxylase from Sulfobacillus acidophilus Strain NY-1 Isolated from Lignite Mines
Received: 2 Feb 2020 Received in revised: 11 Jul 2020 Accepted: 20 Jul 2020 Published online: 18 Aug 2020 DOI: 10.32526/ennrj.18.4.2020.34 One of the key compounds engaged in the carbon dioxide
Structural and Functional Similarities between a Ribulose-1,5-bisphosphate Carboxylase/Oxygenase (RuBisCO)-like Protein from Bacillus subtilis and Photosynthetic RuBisCO*
TLDR
Similarities between the active site structures of RuBisCO and B. subtilis RLP were examined by analyzing the effects of structural analogs of RuBP on DK-MTP-1-P enolase activity, suggesting that the amino acid residues utilized in the B. subtitle RLP enol enzyme reaction are the same as those utilize in the RuBISCO RuBP enolization reaction.
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