Molecular mechanics studies of coenzyme B12 complexes with constrained CoN(axial-base) bond lengths: introduction of the universal force field (UFF) to coenzyme B12 chemistry and its use to probe the plausibility of an axial-base-induced, ground-state corrin butterfly conformational steric effect-Reference-Cited by-同舟云学术

Molecular mechanics studies of coenzyme B12 complexes with constrained CoN(axial-base) bond lengths: introduction of the universal force field (UFF) to coenzyme B12 chemistry and its use to probe the plausibility of an axial-base-induced, ground-state corrin butterfly conformational steric effect

Published:2000-04 Issue: Volume:300-302 Page:545-555
ISSN:0020-1693
Container-title:Inorganica Chimica Acta
language:en
Short-container-title:Inorganica Chimica Acta

Author:

Sirovatka Jeanne M,Rappé Anthony K,Finke Richard G

Publisher

Elsevier BV

Subject

Materials Chemistry,Inorganic Chemistry,Physical and Theoretical Chemistry

Reference73 articles.

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2. B. Kräutler, D. Arigoni, B.T. Golding (Eds.), Vitamin B12 and B12-Proteins, Wiley-VCH, New York, 1998.

3. Thermolysis of adenosylcobalamin: a product, kinetic, and cobalt-carbon (C5') bond dissociation energy study

4. Thermolysis of the CoC bond in adenosylcobalamin (coenzyme B12)—IV. Products, kinetics and CoC bond dissociation energy studies in ethylene glycol

5. Hydrogen abstraction from thiols by adenosyl radicals: chemical precedent for thiyl radical formation, the first catalytic step in ribonucleoside triphosphate reductase from Lactobacillus leichmannii

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