Probing the radical mechanism of galactose oxidase using an ultrafast radical probe.
Processing of trans-2-phenylcyclopropylmethanols 5 and 6 by the monocopper/tyrosine radical enzyme galactose oxidase led to mechanism-based inactivation with a partition ratio, (k(cat) + k(inact))/k(inact), of approximately 1 and a primary deuterium isotope effect, k(inact(H))/k(inact(D)), of 3.2. The data are consistent with a radical mechanism for galactose oxidase with a short lived ketyl radical anion intermediate.
Turner
B E
BE
Department of Chemistry, University of Oregon, Eugene 97403-1253, USA.
Branchaud
B P
BP
D002384:Catalysis; D005692:Galactose Oxidase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D007700:Kinetics; D015335:Molecular Probes
D015335:Molecular Probes; D005692:Galactose Oxidase