Product stabilization in the enzymatic activation of coenzyme B12: a molecular modeling study
Author:
Publisher
Elsevier BV
Subject
Physical and Theoretical Chemistry,Condensed Matter Physics,Biochemistry
Reference63 articles.
1. Activation Parameters for the Carbon−Cobalt Bond Homolysis of Coenzyme B12 Induced by the B12-Dependent Ribonucleotide Reductase from Lactobacillus leichmannii
2. Thermolysis of coenzymes B12 at physiological temperatures: activation parameters for cobalt–carbon bond homolysis and a quantitative analysis of the perturbation of the homolysis equilibrium by the ribonucleoside triphosphate reductase from Lactobacillus leichmannii
3. Thermodynamic and Kinetic Characterization of Co−C Bond Homolysis Catalyzed by Coenzyme B12-Dependent Methylmalonyl-CoA Mutase
4. Enzymatic Radical Catalysis: Coenzyme B12-Dependent Diol Dehydratase
5. Coenzyme B12 Is Coordinated by Histidine and Not Dimethylbenzimidazole on Methylmalonyl-CoA Mutase
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1. Crystal Structures and Coordination Behavior of Aqua- and Cyano-Co(III) Tetradehydrocorrins in the Heme Pocket of Myoglobin;Inorganic Chemistry;2016-01-13
2. Cloning, Expression, Mutagenesis Library Construction of Glycerol Dehydratase, and Binding Mode Simulation of Its Reactivase with Ligands;Applied Biochemistry and Biotechnology;2015-11-07
3. Modeling Enzymatic Reactions in Metalloenzymes and Photobiology by Quantum Mechanics (QM) and Quantum Mechanics/Molecular Mechanics (QM/MM) Calculations;Quantum Biochemistry;2010-06-25
4. Structure and Function: Insights into Bioinorganic Systems from Molecular Mechanics Calculations;Structure and Function;2009-11-05
5. DFT and ONIOM(DFT:MM) Studies on Co−C Bond Cleavage and Hydrogen Transfer in B12-Dependent Methylmalonyl-CoA Mutase. Stepwise or Concerted Mechanism?;Journal of the American Chemical Society;2009-03-23
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