Radical Peregrinations Catalyzed by Coenzyme B12-Dependent Enzymes
Author:
Affiliation:
1. Biochemistry Department, University of Nebraska, Lincoln, Nebraska 68588-0664
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi0104423
Reference73 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 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
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