skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Kinetic investigation of the catalytic mechanism for bovine liver mitochondrial monoamine oxidase

Thesis/Dissertation ·
OSTI ID:5363051

The kinetic behavior of the oxidative deamination reaction catalyzed by bovine liver mitochondrial monoamine oxidase was investigated with a series of ring-substituted benzylamines. Oxidation rates were fastest with the meta isomers. Dalziel coefficients were consistent with a mechanism involving a ternary complex for all substrates tested. Alterations in the Michaelis constant for oxygen were similar in magnitude to those for the rate of catalysis. Deuterium and tritium isotope effects were determined to obtain more detailed information on the mechanism of catalysis. Large deuterium isotope effects expressed on k{sub cat} were obtained for all substrates. Determination of the tritium isotope effect for benzylamine allowed the calculation of an intrinsic isotope effect of 6.5 and a secondary isotope effect of 1.17. Steady-state experiments were supplemented with pre-steady-state kinetic techniques. Rates of flavin reduction were faster than that of turnover. The deuterium isotope effect obtained for the rate of flavin reduction was 7-15 for the various substrates. The observed isotope effect was found to be an appropriate estimate for the intrinsic isotope effect.

Research Organization:
Emory Univ., Atlanta, GA (USA)
OSTI ID:
5363051
Resource Relation:
Other Information: Thesis (Ph. D.)
Country of Publication:
United States
Language:
English