title: Probing the radical mechanism of galactose oxidase using an ultrafast radical probe.
abstract: 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.
authors.affiliation: Department of Chemistry, University of Oregon, Eugene 97403-1253, USA.
authors.forename: B E
authors.initials: BE
authors.lastname: Turner
authors.forename: B P
authors.initials: BP
authors.lastname: Branchaud
mesh_terms: D002384:Catalysis; D005692:Galactose Oxidase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D007700:Kinetics; D015335:Molecular Probes
chemical_list: D015335:Molecular Probes; D005692:Galactose Oxidase