Determination of the structural environment of the tyrosyl radical in prostaglandin H2 synthase-1: A high frequency ENDOR/EPR study

John C. Wilson; Gang Wu; Ah Lim Tsai; Gary J. Gerfen

doi:10.1021/ja043853q

Determination of the structural environment of the tyrosyl radical in prostaglandin H₂ synthase-1: A high frequency ENDOR/EPR study

John C. Wilson, Gang Wu, Ah Lim Tsai, Gary J. Gerfen

Physiology & Biophysics

Research output: Contribution to journal › Article › peer-review

29 Scopus citations

Abstract

The catalytically active tyrosyl radical which gives rise to the "wide doublet" (WD1) signal in ovine Prostaglandin H₂ Synthase-1 has been studied using high frequency (HF) pulsed ENDOR and EPR. A hydrogen-bonded deuteron was directly detected in HFENDOR (130 GHz) spectra of ¹H₂O/²H₂O-exchanged samples. The HFENDOR spectral simulations required a distribution in hydrogen bond distances to achieve proper fits. This range of distances was consistent with that used to model the distribution in g_X values detected in pulsed HFEPR spectra. Possible hydrogen-bonding partners, as well as implications regarding the mechanism of self-inactivation for PGHS, are discussed.

Original language	English (US)
Pages (from-to)	1618-1619
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	127
Issue number	6
DOIs	https://doi.org/10.1021/ja043853q
State	Published - Feb 16 2005

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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Determination of the structural environment of the tyrosyl radical in prostaglandin H₂ synthase-1: A high frequency ENDOR/EPR study

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