TY - JOUR
T1 - Probing the radical mechanism of galactose oxidase using an ultrafast radical probe
AU - Turner, B. Elizabeth
AU - Branchaud, Bruce P.
N1 - Funding Information:
AcknowledgmentT: his researchw as supportedb y NSF GrantM CB-9311514W. e thank Brian Arbogasta t OregonS tateU niversityfo r determinintgh ei sotopicc ompositioonf deuterium-label6e.d
PY - 1999/12/6
Y1 - 1999/12/6
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0033530861&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0033530861&partnerID=8YFLogxK
U2 - 10.1016/S0960-894X(99)00611-3
DO - 10.1016/S0960-894X(99)00611-3
M3 - Article
C2 - 10612596
AN - SCOPUS:0033530861
SN - 0960-894X
VL - 9
SP - 3341
EP - 3346
JO - Bioorganic and Medicinal Chemistry Letters
JF - Bioorganic and Medicinal Chemistry Letters
IS - 23
ER -