Radical Intermediates in the Coenzyme B12 Dependent Methylmalonyl‐CoA Mutase Reaction Shown by ESR Spectroscopy
- 1 February 1992
- journal article
- Published by Wiley in Angewandte Chemie-International Edition
- Vol. 31 (2), 215-216
- https://doi.org/10.1002/anie.199202151
Abstract
No abstract availableKeywords
This publication has 10 references indexed in Scilit:
- Vitamin B12S-promoted model rearrangement of methylmalonate to succinate is not a free radical reaction.Proceedings of the National Academy of Sciences, 1990
- 1,2-Migrations in free radicals related to coenzyme B12-dependent rearrangementsJournal of the American Chemical Society, 1988
- Free radical rearrangement involving the 1,2-migration of a thioester group. Model for the coenzyme B12-dependent methylmalonyl-CoA mutase reactionJournal of the American Chemical Society, 1984
- Review of the EPR of B12r and B12 -dependent enzyme reactionsPublished by Walter de Gruyter GmbH ,1979
- A physical explanation of the EPR spectrum observed during catalysis by enzymes utilizing coenzyme BBiochimica et Biophysica Acta (BBA) - Enzymology, 1975
- The Mechanism of Action of Ethanolamine Ammonia-Lyase, a B12-dependent EnzymePublished by Elsevier BV ,1974
- Cobamides and Ribonucleotide ReductionPublished by Elsevier BV ,1974
- Electron Spin Resonance Studies with DioldehydraseJournal of Biological Chemistry, 1973
- The Mechanism of Action of Ethanolamine Ammonia Lyase, a B12-dependent EnzymePublished by Elsevier BV ,1972
- Detection of intermediates during the conversion of propane-1,2-diol to propionaldehyde by glycerol dehydrase, a coenzyme B12-dependent reactionJournal of the American Chemical Society, 1972