Modification of ribulose bisphosphate carboxylase from Rhodospirillumrubrum with tetranitromethane
Biochemical and Biophysical Research Communications, 1979Abstract Ribulose bisphosphate carboxylase from Rhodospirillum rubrum is inactivated by low concentrations of tetranitromethane. Addition of the substrate ribulose 1,5-bisphosphate and preincubation with Mg+2 and HCO 3 − both protect against inactivation.
P D, Robison, F R, Tabita
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Regulation of activation of ribulose bisphosphate carboxylase from Pseudomonasoxalaticus
Biochemical and Biophysical Research Communications, 1978Abstract 6-phosphogluconate, potentiated activation of ribulose bisphosphate carboxylase from Pseudomonas oxalaticus whereas fructose-1,6-bisphosphate inhibited activation and fructose-6-phosphate had no effect. The presence of 1 mM 6-phosphogluconate during activation reduced the Kact for Mg2+ from 1.4 mM to approximately 0.2 mM.
V B, Lawlis, G L, Gordon, B A, McFadden
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Some Mechanistic Aspects of Ribulose Bisphosphate Carboxylase
1984Water is involved in the carboxylase reaction in 2 distinct ways (Fig 1.) Besides its stoichiometric involvement, it hydrates both substrates. While carbon dioxide has long been recognised as the active species, no information is yet available on how the enzyme handles the geM-diol form of RuBP.
George H. Lorimer +3 more
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Comparative Biochemistry of Ribulose Bisphosphate Carboxylase in Higher Plants
1978The agronomically important aspects of the comparative biochemistry of RuBP carboxylase are locating a natural enzyme, creating a mutant enzyme, or identifying compounds which differentially alter the enzyme so as to allow CO2 to be fixed more efficiently or O2 to be fixed less efficiently.
W L, Ogren, L D, Hunt
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Stoichiometry in the assay of ribulose bisphosphate oxygenase and carboxylase
Analytical Biochemistry, 1982Abstract Complete stoichiometry of the reaction catalyzed by ribulose 1,5-bisphosphate (RuBP) oxygenase from spinach and Rhodospirillum rubrum has been determined. Before initiation and after termination, RuBP has been measured either by release of equimolar orthophosphate at 25°C in the presence of 1 n NaOH or by complete carboxylation using 14CO2
K, Purohit, B A, McFadden, A, Saluja
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Reversible dissociation and conformational stability of dimeric ribulose bisphosphate carboxylase
Biochemistry, 1993Dimer-monomer dissociation of ribulosebisphosphate carboxylase/oxygenase from Rhodospirillum rubrum was investigated using hydrostatic pressure in the range 1-2 kbar to promote dissociation. Intrinsic fluorescence emission and polarization, along with the polarization of the fluorescence of single-labeled AEDANS conjugates, were used to follow the ...
L, Erijman, G H, Lorimer, G, Weber
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Ribulose bisphosphate carboxylase—oxygenase: its role in photosynthesis
Philosophical Transactions of the Royal Society of London. B, Biological Sciences, 1986Synthesis of triose phosphate by the chloroplast requires three substrates: light, CO2and orthophosphate (Pi). In the response of the rate of carbon assimilation to the concentration of CO2, the kinetic properties of RuBP carboxylase-oxygenase (Rubisco) constitute the main limitation at low CO2concentrations, while at higher concentrations of CO2the ...
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The Active Site of Ribulose Bisphosphate Carboxylase / Oxygenase
1990Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) has attracted a lot of interest due to its central role in the carbon metabolism of plants and photosynthetic microorganisms (for a review see (1)). The dual function of this enzyme, catalyzing the primary steps in both photosynthetic carbon dioxide fixation and photorespiration, makes it a ...
G. Schneider, Y. Lindqvist, T. Lundqvist
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Radiochemical assay of ribulose bisphosphate carboxylase
Biochemical Education, 1989Carl S. Pike, Joseph A. Berry
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Fibroblast pyruvate carboxylase is required for collagen production in the tumour microenvironment
Nature Metabolism, 2021Simon Schwörer +2 more
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