Evidence from Electron Paramagnetic Resonance Spectroscopy of the Participation of Radical Intermediates in the Reaction Catalyzed by Methylmalonyl-coenzyme A Mutase-Reference-Cited by-同舟云学术

Evidence from Electron Paramagnetic Resonance Spectroscopy of the Participation of Radical Intermediates in the Reaction Catalyzed by Methylmalonyl-coenzyme A Mutase

Published:1995-04 Issue:16 Volume:270 Page:9295-9300
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Padmakumar Rugmini,Banerjee Ruma

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference38 articles.

1. The Natural History of the Inherited Methylmalonic Acidemias

2. PURIFICATION AND PROPERTIES OF ENZYMES INVOLVED IN THE PROPIONIC ACID FERMENTATION

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. Vitamin B12S-promoted model rearrangement of methylmalonate to succinate is not a free radical reaction.

5. First hydrogen abstraction-rearrangement model for the coenzyme B12-dependent methylmalonyl-CoA to succinyl-CoA carbon skeleton rearrangement reaction

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