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Structure and function of Rubisco
Plant Physiology and Biochemistry, 2008Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the major enzyme assimilating CO(2) into the biosphere. At the same time Rubisco is an extremely inefficient catalyst and its carboxylase activity is compromised by an opposing oxygenase activity involving atmospheric O(2).
Anders Backlund, Inger Andersson
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Rubisco activase - Rubisco's catalytic chaperone.
Photosynthesis research, 2003The current status of research on the structure, regulation, mechanism and importance of Rubisco activase is reviewed. The activase is now recognized to be a member of the AAA(+) family, whose members participate in macromolecular complexes that perform diverse chaperone-like functions.
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Protein engineering of rubisco
Acta Crystallographica Section B Structural Science, 1991Modification of the kinetic parameters of enzymes by protein engineering requires extensive knowledge of the structural details of the enzyme and its complexes with different reaction intermediate analogues. Such structural studies are described here for Rubisco, ribulose-1,5-bisphosphate carboxylase/oxygenase, which catalyzes the initial reactions of ...
C I Brändén +2 more
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Rubisco: Structure and Mechanism
Annual Review of Biophysics and Biomolecular Structure, 1992CONTENTS PERSPECTIVES AND OVERVIEW 1 1 9 PHYSIOLOGICAL AND GENETIC ASPECTS 120 Photosynthesis and Photorespiration 120 Synthesis and Assembly . . . . . ..... ... . . ... . . . . . . . . . . .. .. 121 CHEMICAL MECHANISM 122 Activation-the Ternary Complex of Enzyme, CO" and Mg( II) 122 Overall Carboxylation Reaction . . . ... . . . . . .
Gunter Schneider +2 more
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Photosynthesis: Rubisco rescue
Nature Plants, 2015Rubisco catalyses the first step in photosynthetic carbon fixation, but it can be easily poisoned by side-products of its activity. Structural and functional analyses of a protein conserved across plants, algae and bacteria shows how one such blockage is both removed and recycled.
Rebekka M. Wachter, J. Nathan Henderson
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Maximum Carboxylation Rate Estimation With Chlorophyll Content as a Proxy of Rubisco Content
Journal of Geophysical Research: Biogeosciences, 2020The maximum carboxylation rate (Vcmax) is a key parameter in determining the plant photosynthesis rate per unit leaf area. However, most terrestrial biosphere models currently treat Vcmax as constants changing only with plant functional types, leading to
Xuehe Lu +7 more
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Rubisco: Maladapted or Misunderstood
Australian Journal of Botany, 1992Life depends on a single enzyme, D-ribulose-1,5-bisphosphate carboxylase-oxygenase (Rubisco), for the acquisition of essentially all of its carbon. Applying Darwinian principles, one would expect this enzyme to have been rigorously selected for speed and accuracy, and it is a surprise to discover that, even in its most highly developed forms, it is ...
K Paul +3 more
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1983
Leaf rubisco (Fraction 1 protein) was purified from a number of cruciferous species, and subunit polypeptide patterns were examined by isoelectric focusing in the presence of 8 M urea. Both cultivated and wild Brassica species were studied by this method and results suggest that the protein may be a useful taxonomic marker, especially where species may
M. P. Robbins, J. G. Vaughan
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Leaf rubisco (Fraction 1 protein) was purified from a number of cruciferous species, and subunit polypeptide patterns were examined by isoelectric focusing in the presence of 8 M urea. Both cultivated and wild Brassica species were studied by this method and results suggest that the protein may be a useful taxonomic marker, especially where species may
M. P. Robbins, J. G. Vaughan
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Evolution and origins of rubisco
Current BiologyRubisco (D-ribulose 1,5-bisphosphate carboxylase/oxygenase) is the most abundant enzyme in the world, constituting up to half of the soluble protein content in plant leaves. Such is its ubiquity that its chemical fingerprint can be detected in the geological record spanning billions of years.
Leah J, Taylor-Kearney +2 more
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