Spectroscopic and Computational Studies on the Adenosylcobalamin-Dependent Methylmalonyl-CoA Mutase:  Evaluation of Enzymatic Contributions to Co−C Bond Activation in the Co3+ Ground State

• Published in: Journal of the American Chemical Society Vol. 126; no. 26; pp. 8167 - 8180
• Main Authors: Brooks, Amanda J, Vlasie, Monica, Banerjee, Ruma, Brunold, Thomas C
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 07.07.2004
• Subjects: Binding Sites; Biological and medical sciences; Circular Dichroism; Cobalt - chemistry; Cobamides - chemistry; Fundamental and applied biological sciences. Psychology; Interactions. Associations; Intermolecular phenomena; Magnetic Resonance Spectroscopy; Methylmalonyl-CoA Mutase - chemistry; Models, Chemical; Molecular biophysics; Molecular Structure; Substrate Specificity; MO method; Frontier orbital; Enzyme; Theoretical study; Electron charge distribution; Molecular interaction; Experimental study; Magnetic circular dichroism spectrometry; Electronic structure; Isomerases; Binding capacity; Intramolecular transferases; Molecular association; Density functional method; Potential energy surfaces; Local density approximation; Methylmalonyl-CoA mutase
• ISSN: 0002-7863; 1520-5126
• DOI: 10.1021/ja039114b

Methylmalonyl-CoA mutase (MMCM) is an enzyme that utilizes the adenosylcobalamin (AdoCbl) cofactor to catalyze the rearrangement of methylmalonyl-CoA to succinyl-CoA. Despite many years of dedicated research, the mechanism by which MMCM and related AdoCbl-dependent enzymes accelerate the rate for ho...