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Magnetic field effects on coenzyme B 12 ‐dependent enzymes: Validation of ethanolamine ammonia lyase results and extension to human methylmalonyl CoA mutase
Author(s) -
Taoka Shinichi,
Padmakumar Raghavakaimal,
Grissom Charles B.,
Banerjee Ruma
Publication year - 1997
Publication title -
bioelectromagnetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.435
H-Index - 81
eISSN - 1521-186X
pISSN - 0197-8462
DOI - 10.1002/(sici)1521-186x(1997)18:7<506::aid-bem6>3.0.co;2-6
Subject(s) - mutase , chemistry , ethanolamine , enzyme , cofactor , lyase , biochemistry , corrin , stereochemistry , vitamin b12
Enzymes with radical‐pair intermediates have been considered as a likely target for purported magnetic field effects in humans. The bacterial enzyme ethanolamine ammonia lyase and the human enzyme methylmalonyl‐CoA mutase catalyze coenzyme B 12 ‐dependent rearrangement reactions. A common step in the mechanism of these two enzymes is postulated to be homolysis of the cobalt‐carbon bond of the cofactor to generate a spin‐correlated radical pair consisting of the 5′‐deoxyadenosyl radical and cob(II)alamin [Ado · Cbl(II)]. Thus, the reactions catalyzed by these enzymes are expected to be sensitive to an applied magnetic field according to the same principles that control radical pair chemical reactions. The magnetic field effect on ethanolamine ammonia lyase reported previously has been corroborated independently in one of the authors' laboratory. However, neither the human nor the bacterial mutase from Propionibacterium shermanii exhibits a magnetic field effect that could be greater than about 15%, considering the error limit imposed by the uncertainty of the coupled assay. Our studies suggest that putative magnetic field effects on physiological processes are not likely to be mediated by methylmalonyl‐CoA mutase. Bioelectromagnetics 18:506–513, 1997. © 1997 Wiley‐Liss, Inc.