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J Biol Chem, Vol. 274, Issue 14, 9231-9237, April 2, 1999
From the Prostaglandin H synthase (PGHS) is a
self-activating and self-inactivating enzyme. Both the peroxidase and
cyclooxygenase activities have a limited number of catalytic turnovers.
Sequential stopped-flow measurements were used to analyze the kinetics
of PGHS-1 peroxidase self-inactivation during reaction with several different hydroperoxides. The inactivation followed single exponential kinetics, with a first-order rate constant of 0.2-0.5
s
A Mechanistic Study of Self-inactivation of the Peroxidase
Activity in Prostaglandin H Synthase-1
,,,
Division of Hematology, Department of
Internal Medicine, University of Texas Health Science Center,
Houston, Texas 77030 and the § Department of Pharmacology,
University of Michigan Medical School,
Ann Arbor, Michigan 48109-0632
1 at 24 °C. This rate was independent of the
peroxide species and concentration used, strongly suggesting that the
self-inactivation process originates after formation of Compound I and
probably with Intermediate II, which contains an oxyferryl heme and a
tyrosyl radical. Kinetic scan and rapid scan experiments were used to monitor the heme changes during the inactivation process. The results
from both experiments converged to a simple, linear, two-step mechanism
in which Intermediate II is first converted in a faster step (0.5-2
s1) to a new compound, Intermediate III, which undergoes
a subsequent slower (0.01-0.05 s1) transition to a
terminal species. Rapid-quench and high pressure liquid chromatography
analysis indicated that Intermediate III likely retains an intact heme
group that is not covalently linked with the PGHS-1 protein.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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