Adenosylcobinamide Plus Exogenous, Sterically Hindered, Putative Axial Bases: A Reinvestigation into the Cause of Record Levels of Co−C Heterolysis-Reference-Cited by-同舟云学术

Adenosylcobinamide Plus Exogenous, Sterically Hindered, Putative Axial Bases: A Reinvestigation into the Cause of Record Levels of Co−C Heterolysis

Published:2004-03-19 Issue:8 Volume:43 Page:2611-2623
ISSN:0020-1669
Container-title:Inorganic Chemistry
language:en
Short-container-title:Inorg. Chem.

Author:

Doll Kenneth M.¹,Finke Richard G.¹

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/ic030141c

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2. Sirovatka, J. M. Chemical Precedent Studies for the Mechanism of Adenosylcobalamin-Dependent Enzymes. Ph.D. Thesis, Colorado State University, Chemistry, 1999.

3. 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.

4. Studies on the Mechanism of the Reaction between Coenzyme B12 and Cyanide: Direct 1H NMR Spectroscopic Evidence for a (β-5‘-Deoxyadenosyl)(α-cyano)cobalamin Intermediate

5. 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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