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Peroxide-induced radical formation at TYR385 and TYR504 in human PGHS-1.

Journal of inorganic biochemistry - 1 Jun 2009

Rogge Corina E, Liu Wen, Kulmacz Richard J, Tsai Ah-Lim

Abstract excerpt

Prostaglandin H synthase isoforms 1 and -2 (PGHS-1 and -2) react with peroxide to form a radical on Tyr385 that initiates the cyclooxygenase catalysis. The tyrosyl radical EPR signals of PGHS-1 and -2 change over time and are altered by cyclooxygenase inhibitor binding. We characterized the tyrosyl radical dynamics using wild type human PGHS-1 (hPGHS-1) and its Y504F, Y385F, and Y385F/Y504F mutants to determine...

Topics

Arachidonic Acid
Catalysis
Cyclooxygenase 1
Cyclooxygenase 2
Electron Spin Resonance Spectroscopy
Free Radicals
Humans
Hydrogen Peroxide
Kinetics
Mutation
Tyrosine

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Identifiers

PMID: 19433337
DOI: 10.1016/j.jinorgbio.2009.04.002
PMCID: PMC2697118

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