Conformational studies of 5′-deoxyadenosyl-13-epicobalamin, a coenzymatically active structural analog of coenzyme B12
Author:
Publisher
Elsevier BV
Subject
Materials Chemistry,Inorganic Chemistry,Physical and Theoretical Chemistry
Reference72 articles.
1. Thermolysis of adenosylcobalamin: a product, kinetic, and cobalt-carbon (C5') bond dissociation energy study
2. Thermolysis of the cobalt-carbon bond of adenosylcobalamin. 2. Products, kinetics, and cobalt-carbon bond dissociation energy in aqueous solution
3. 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
4. Side Chain Entropy and the Activation of Organocobalamins for Carbon−Cobalt Bond Homolysis: Synthesis, Characterization, and Thermolysis of the Neopentyl Derivative of a Unique Cobalamin Analog Lacking a c Side Chain
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2. Large-Scale Domain Conformational Change Is Coupled to the Activation of the Co–C Bond in the B12-Dependent Enzyme Ornithine 4,5-Aminomutase: A Computational Study;Journal of the American Chemical Society;2012-01-19
3. Large-scale Domain Dynamics and Adenosylcobalamin Reorientation Orchestrate Radical Catalysis in Ornithine 4,5-Aminomutase;Journal of Biological Chemistry;2010-04
4. Structure and Function: Insights into Bioinorganic Systems from Molecular Mechanics Calculations;Structure and Function;2009-11-05
5. NMR spectroscopy and molecular modelling studies of nitrosylcobalamin: further evidence that the deprotonated, base-off form is important for nitrosylcobalamin in solution;Dalton Trans.;2009
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