MAGNETIC-FIELD EFFECTS ON B-12 ETHANOLAMINE AMMONIA-LYASE - EVIDENCE FOR A RADICAL MECHANISM

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 V-max/K-m (where K-m is the Michaelis constant) for the coenzyme B-12-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.