Oxygen metabolism by endothelial nitric-oxide synthase.

Oxygen metabolism by endothelial nitric-oxide synthase. Research Abstract Details 

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Oxygen metabolism by endothelial nitric-oxide synthase. Abstract Text:

Ying Tong Gao,Linda J Roman,Pavel ,Satya Prakash Panda,Yuzuru Ishimura,Bettie Sue S Masters,

Nitric-oxide synthase (NOS) catalyzes both coupled and uncoupled reactions that generate nitric oxide and reactive oxygen species. Oxygen is often the overlooked substrate, and the oxygen metabolism catalyzed by NOS has been poorly defined. In this paper we focus on the oxygen stoichiometry and effects of substrate/cofactor binding on the endothelial NOS isoform (eNOS). In the presence of both L-arginine and tetrahydrobiopterin, eNOS is highly coupled (>90%), and the measured stoichiometry of O(2)/NADPH is very close to the theoretical value. We report for the first time that the presence of L-arginine stimulates oxygen uptake by eNOS. The fact that nonhydrolyzable L-arginine analogs are not stimulatory indicates that the occurrence of the coupled reaction, rather than the accelerated uncoupled reaction, is responsible for the L-arginine-dependent stimulation. The presence of 5,6,7,8-tetrahydrobiopterin quenched the uncoupled reactions and resulted in much less reactive oxygen species formation, whereas the presence of redox-incompetent 7,8-dihydrobiopterin demonstrates little quenching effect. These results reveal different mechanisms for oxygen metabolism for eNOS as opposed to nNOS and, perhaps, partially explain their functional differences.

Oxygen metabolism by endothelial nitric-oxide synthase. Publishing Authors By Initials

YT Gao,LJ Roman,P ,SP Panda,Y Ishimura,BS Masters,

For similar proteins: recombinant proteins research abstracts see: proteins: recombinant proteins research

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Oxygen metabolism by endothelial nitric-oxide synthase. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: The Journal of biological chemistry

VOLUME: 282

Page Numbers: 28557-65

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 13

MONTH: 08

YEAR: 2007

Oxygen metabolism by endothelial nitric-oxide synthase. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

Oxygen metabolism by endothelial nitric-oxide synthase. Keywords Mesh Terms:

KEYWORDS: Recombinant Proteins

MESH TERMS: metabolism

Chemical & Substance for Abstract: Oxygen metabolism by endothelial nitric-oxide synthase. Information

Substance Name: Nitric Oxide Synthase Type III

Registry Number: EC 1.14.13.39

Grant and Affiliation Information for Oxygen metabolism by endothelial nitric-oxide synthase.

AFFILIATION: Department of Biochemistry, The University of Texas Health Science Center at San Antonio, San Antonio, Texas 78229-3900, USA.

Country: United States

AGENCY: United States NHLBI

GRANT: HL30050

ACRONYM: HL

MEDLINETA: J Biol Chem

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