Identification of two binding sites of the d-ribulose 1,5-bisphosphate carboxylase/oxygenase from spinach for d-ribulose 1,5-bisphosphate and effectors of the carboxylation reaction
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference13 articles.
1. Activation and Inhibition of Ribulose 1,5-Diphosphate Carboxylase by 6-Phosphogluconate
2. The activation of ribulose-1,5-bisphosphate carboxylase by carbon dioxide and magnesium ions. Equilibria, kinetics, a suggested mechanism, and physiological implications
3. A model for the kinetics of activation and catalysis of ribulose 1,5-bisphosphate carboxylase
4. Regulation of Ribulose 1,5-Diphosphate Carboxylase by Substrates and Other Metabolites
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1. Identification of Interactions between Abscisic Acid and Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase;PLOS ONE;2015-07-21
2. Crystal Structure of Rice Rubisco and Implications for Activation Induced by Positive Effectors NADPH and 6-Phosphogluconate;Journal of Molecular Biology;2012-09
3. Determining RuBisCO activation kinetics and other rate and equilibrium constants by simultaneous multiple non-linear regression of a kinetic model;Journal of Experimental Botany;2006-10-17
4. Microcalorimetric determination of the reaction enthalpy changes associated with the carboxylase and oxygenase reactions catalysed by ribulose 1,5-bisphosphate carboxylase/oxygenase (RUBISCO);Physical Chemistry Chemical Physics;2000
5. Thermodynamics and kinetics of sugar phosphate binding to D-ribulose 1,5-bisphosphate carboxylase/oxygenase (RUBISCO);Journal of the Chemical Society, Faraday Transactions;1998
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