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

  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},
  • 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. 

The Hidden Face of Rubisco.

Slow deactivation of ribulose 1,5‐bisphosphate carboxylase/oxygenase elucidated by mathematical models

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.

Rubisco regulation: a role for inhibitors.

The regulation ofRubisco activity in higher plants is reviewed here, including the role of Rubisco activase, tight binding inhibitors, and the impact of abiotic stress upon them.

Slow deactivation of RuBisCO elucidated by mathematical models

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.

Role of auxiliary proteins in Rubisco biogenesis and function

An integrated view of the pathways underlying Rubisco biogenesis and repair will pave the way for efforts to improve the enzyme with the goal of increasing crop yields.

From chaperonins to Rubisco assembly and metabolic repair

  • M. Hayer‐Hartl
  • Biology, Environmental Science
    Protein science : a publication of the Protein Society
  • 2017
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*

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.

Chapter 6 Photorespiration: The Bridge to C4 Photosynthesis

Photorespiration is one of the major highways of carbon metabolism in C3 plants and hence in the biogeosphere. By mass flow, excelled only by photosynthesis, it actually constitutes the second-most



Along the trail from Fraction I protein to Rubisco (ribulose bisphosphate carboxylase-oxygenase)

  • S. Wildman
  • Environmental Science
    Photosynthesis Research
  • 2004
This historical minireview deals with events leading to the eventual discovery of Rubisco (ribulose bisphosphate carboxylase-oxygenase). This abundant leaf protein is not only responsible for the net

Ribulose-1,5-diphosphate carboxylase and oxygenase from green plants are two different enzymes.

  • R. Brändén
  • Biology, Physics
    Biochemical and biophysical research communications
  • 1978

Regulation of RuDP carboxylase/oxygenase activity and its relationship to plant photorespiration

The ribulose 1,5-diphosphate carboxylase/oxygenase function has been suggested to be the primary source of phosphogly-colate, the principal substrate for photorespiration5.

Molecular diversity of the ribulose-1,5-diphosphate carboxylase from photosynthetic microorganisms.

The ribulose-1,5-diphosphate carboxylases from green and blue-green algae and the purple sulfur photosynthetic bacterium Chromatium are proteins with high molecular weights and with sedimentation

Ribulose-1, 5-diphosphate from and CO2 fixation by Tetragonia expansa leaves extract.

L-3-phosphoglyceric acid, formed by ribulose-1,5-bisphosphate carboxylase, is the primary substrate for photorespiration: experimental test of a hypothesis.

Microbial ribulose 1,5-bisphosphate carboxylase/oxygenase: A different perspective

This review considers the major issues of Rubisco biochemistry and regulation in photosynthetic microoganisms including proteob bacteria, cyanobacteria, marine nongreen algae, as well as other interesting prokaryotic and eukaryotic microbial systems recently shown to possess this enzyme.

Rubisco: Maladapted or misunderstood?

The possibilities for improving Rubisco artificially, either by random mutagenesis or by rational design, are assessed and the consequences of an improved Rubisco for plant productivity and the global ecosystem are imagined.