title: Magnetic field effects on B12 ethanolamine ammonia lyase: evidence for a radical mechanism.
abstract: A change in radical pair recombination rates is one of the few mechanisms by which a magnetic field can interact with a biological system. The kinetic parameter Vmax/Km (where Km is the Michaelis constant) for the coenzyme B12-dependent enzyme ethanolamine ammonia lyase was decreased 25 percent by a static magnetic field near 0.1 tesla (1000 gauss) with unlabeled ethanolamine and decreased 60 percent near 0.15 tesla with perdeuterated ethanolamine. This effect is likely caused by a magnetic field-induced change in intersystem crossing rates between the singlet and triplet spin states in the [cob(II)alamin:5'-deoxyadenosyl radical] spin-correlated radical pair.
authors.affiliation: Department of Chemistry, University of Utah, Salt Lake City 84112.
authors.forename: T T
authors.initials: TT
authors.lastname: Harkins
authors.forename: C B
authors.initials: CB
authors.lastname: Grissom
mesh_terms: D003903:Deuterium; D019856:Ethanolamine; D004981:Ethanolamine Ammonia-Lyase / Q000378:metabolism*; D004983:Ethanolamines / Q000378:metabolism; D007700:Kinetics; D008280:Magnetics; D010782:Photolysis; D014805:Vitamin B 12 / Q000494:pharmacology
chemical_list: D004983:Ethanolamines; D019856:Ethanolamine; D003903:Deuterium; D004981:Ethanolamine Ammonia-Lyase; D014805:Vitamin B 12