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Tetrahydrobiopterin in nitric oxide synthase†
Article first published online: 26 FEB 2013
Copyright © 2013 International Union of Biochemistry and Molecular Biology, Inc.
Volume 65, Issue 4, pages 358–365, April 2013
How to Cite
Tejero, J. and Stuehr, D. (2013), Tetrahydrobiopterin in nitric oxide synthase . IUBMB Life, 65: 358–365. doi: 10.1002/iub.1136
Abbreviations: CaM, calmodulin; eNOS, endothelial nitric oxide synthase; FAD, flavin adenine dinucleotide; FMN, flavin mononucleotide; H2B, 7,8-dihydrobiopterin; H4B, (6R-)5,6,7,8-tetrahydrobiopterin; H4F, tetrahydrofolate; iNOS, inducible nitric oxide synthase; NADPH, nicotinamide adenine dinucleotide phosphate; nNOS, neuronal nitric oxide synthase; NOHA, Nω-hydroxy arginine; NOS, nitric oxide synthase
- Issue published online: 18 MAR 2013
- Article first published online: 26 FEB 2013
- Manuscript Accepted: 25 DEC 2012
- Manuscript Received: 7 DEC 2012
- nitric oxide synthase;
- nitric oxide;
- pterin radicals;
Summary: Nitric oxide synthase (NOS) is a critical enzyme for the production of the messenger molecule nitric oxide (NO) from L-arginine. NOS enzymes require tetrahydrobiopterin as a cofactor for NO synthesis. Besides being one of the few enzymes to use this cofactor, the role of tetrahydrobiopterin in NOS catalytic mechanism is different from other enzymes: during the catalytic cycle of NOS, tetrahydrobiopterin forms a radical species that is again reduced, thus effectively regenerating after each NO synthesis cycle. In this review, we summarize our current knowledge about the role of tetrahydrobiopterin in the structure, function, and catalytic mechanism of NOS enzymes. © 2013 IUBMB Life 65(4):358–365, 2013.