Importance of the Histidine Ligand to Coenzyme B12 in the Reaction Catalyzed by Methylmalonyl-CoA Mutase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference38 articles.
1. Neopentylcobalamin (neopentylB12) cobalt-carbon bond thermolysis products, kinetics, activation parameters, and bond dissociation energy: a chemical model exhibiting 106 of the 1012 enzymic activation of coenzyme B12's cobalt-carbon bond
2. Thermolysis of the cobalt-carbon bond in adenosylcorrins. 3. Quantification of the axial base effect in adenosylcobalamin by the synthesis and thermolysis of axial base-free adenosylcobinamide. Insights into the energetics of enzyme-assisted cobalt-carbon bond homolysis
3. Radical Peregrinations Catalyzed by Coenzyme B12-Dependent Enzymes
4. Thermodynamic and Kinetic Characterization of Co−C Bond Homolysis Catalyzed by Coenzyme B12-Dependent Methylmalonyl-CoA Mutase
5. Structure of the 5,6-Dimethylbenzimidazolylcobamide Coenzyme
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3. Electron Spin Echo Envelope Modulation Spectroscopy Reveals How Adenosylcobalamin-Dependent Lysine 5,6-Aminomutase Positions the Radical Pair Intermediates and Modulates Their Stabilities for Efficient Catalysis;ACS Catalysis;2021-11-12
4. Cooperative Binding of 1-Phenylimidazole to Cobalt(II) Octaethylporphyrin on Graphite: A Quantitative Imaging and Computational Study at Molecular Resolution;The Journal of Physical Chemistry C;2020-07-29
5. New Insights Into the Biosynthesis of Cobamides and Their Use;Comprehensive Natural Products III;2020
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