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Originally published In Press as doi:10.1074/jbc.M200853200 on August 14, 2002

J. Biol. Chem., Vol. 277, Issue 43, 40275-40280, October 25, 2002
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The Role of Tetrahydrobiopterin in the Regulation of Neuronal Nitric-oxide Synthase-generated Superoxide*

Gerald M. RosenDagger §, Pei TsaiDagger , John Weaver||, Supatra Porasuphatana**, Linda J. RomanDagger Dagger , Anatoly A. Starkov§§, Gary Fiskum§§, and Sovitj PouDagger

From the Dagger  Department of Pharmaceutical Sciences, University of Maryland School of Pharmacy, Baltimore, Maryland 21201 and the Medical Biotechnology Center, University of Maryland Biotechnology Institute, Baltimore, Maryland 21201, the § Center for Low Frequency EPR for in Vivo Physiology, University of Maryland School of Pharmacy, Baltimore, Maryland 21201, the || Department of Chemistry, University of Maryland Baltimore County, Baltimore, Maryland 21250, the ** Department of Toxicology, Faculty of Pharmaceutical Science, Khon Kaen University, Khon Kaen 40002, Thailand, the Dagger Dagger  Department of Biochemistry, The University of Texas Health Science Center, San Antonio, Texas 78229, and the §§ Department of Anesthesiology, University of Maryland School of Medicine, Baltimore, Maryland 21201

Tetrahydrobiopterin (H4B) is a critical element in the nitric-oxide synthase (NOS) metabolism of L-arginine to L-citrulline and NO·. It has been hypothesized that in the absence of or under nonsaturating levels of L-arginine where O2 reduction is the primary outcome of NOS activation, H4B promotes the generation of H2O2 at the expense of O<UP><SUB>2</SUB><SUP>&cjs1138;</SUP></UP>. The experiments were designed to test this hypothesis. To test this theory, two different enzyme preparations, H4B-bound NOS I and H4B-free NOS I, were used. Initial rates of NADPH turnover and O2 utilization were found to be considerably greater in the H4B-bound NOS I preparation than in the H4B-free NOS I preparation. In contrast, the initial generation of O<UP><SUB>2</SUB><SUP>&cjs1138;</SUP></UP> from the H4B-free NOS I preparation was found to be substantially greater than that measured using the H4B-bound NOS I preparation. Finally, by spin trapping nearly all of the NOS I produced O<UP><SUB>2</SUB><SUP>&cjs1138;</SUP></UP>, we found that the initial rate of H2O2 production by H4B-bound NOS I was considerably greater than that for H4B-free NOS I.

* This work was supported in part by National Institutes of Health Grants RR-12257 (to G. M. R.), T32-ES07263 (to P. T.), R25-GM-55036 (to J. W.), NS-34152 (to G. F.), and GM-52419 and Robert A. Welch Foundation Grant AQ1192.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Univ. of Maryland School of Pharmacy, 725 West Lombard St., Baltimore, MD 21201. Tel.: 410-706-0514; Fax: 410-706-8184; E-mail: grosen@umaryland.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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