Coenzyme B12 Axial-Base Chemical Precedent Studies. Adenosylcobinamide Plus Sterically Hindered Axial-Base Co−C Bond Cleavage Product and Kinetic Studies: Evidence for the Dominance of Axial-Base Transition-State Effects and for Co−N(Axial-Base) Distance-Dependent, Competing σ and π Effects
Author:
Affiliation:
1. Department of Chemistry, Colorado State University, Fort Collins, Colorado 80523
Publisher
American Chemical Society (ACS)
Subject
Inorganic Chemistry,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/ic980608x
Reference62 articles.
1. How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2 å resolution
2. Extended X-ray Absorption Fine Structure Analysis of Coenzyme B12 Bound to Methylmalonyl-Coenzyme A Mutase Using Global Mapping Techniques
3. How a Protein Binds B 12 : A 3.0 Å X-Ray Structure of B 12 -Binding Domains of Methionine Synthase
4. Adenosylcobinamide, the Base-Free Analog of Coenzyme B12 (Adenosylcobalamin). 1.1 Probing the Role of the Axial 5,6-Dimethylbenzimidazole Base in Coenzyme B12 via Exogenous Axial Base Kassociation, ΔH, and ΔS Measurements plus a Critical Review of the Relevant Biochemical Literature
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