TY - JOUR
T1 - Intramolecular determination of primary kinetic isotope effects in hydroxylations catalyzed by cytochrome P-450
AU - Hjelmeland, Leonard M
AU - Aronow, Lewis
AU - Trudell, James R.
PY - 1977/5/23
Y1 - 1977/5/23
N2 - Isotope effects for hydroxylation reactions catalyzed by cytochrome P-450 have usually been measured by comparing the overall reaction velocities of deuterated and nondeuterated substrates. Since the rate-limiting step is probably not the single reaction involving covalent bond cleavage, such an approach does not yield information about the primary isotope effect. We measured the primary kinetic isotope effect for benzylic hydroxylation by a method utilizing intramolecular competition, using the symmetrical substrate 1,3-diphenylpropane-1,1-d2. These experiments yield a value of kH kD = 11, a larger effect than has previously been reported for benzylic hydroxylations.
AB - Isotope effects for hydroxylation reactions catalyzed by cytochrome P-450 have usually been measured by comparing the overall reaction velocities of deuterated and nondeuterated substrates. Since the rate-limiting step is probably not the single reaction involving covalent bond cleavage, such an approach does not yield information about the primary isotope effect. We measured the primary kinetic isotope effect for benzylic hydroxylation by a method utilizing intramolecular competition, using the symmetrical substrate 1,3-diphenylpropane-1,1-d2. These experiments yield a value of kH kD = 11, a larger effect than has previously been reported for benzylic hydroxylations.
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U2 - 10.1016/0006-291X(77)90758-6
DO - 10.1016/0006-291X(77)90758-6
M3 - Article
C2 - 1027445
AN - SCOPUS:0017392344
VL - 76
SP - 541
EP - 549
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -