C. Nathan and M. U. Shiloh, Reactive oxygen and nitrogen intermediates in the relationship between mammalian hosts and microbial pathogens, Proceedings of the National Academy of Sciences, vol.97, issue.16, pp.8841-8848, 2000.
DOI : 10.1073/pnas.97.16.8841

H. Stopper, M. Moller, H. M. Bommel, and H. H. Schmidt, Cytotoxic versus genotoxic effects of nitric oxide (NO), Toxicology Letters, vol.106, issue.1, pp.59-67, 1999.
DOI : 10.1016/S0378-4274(99)00019-3

W. K. Alderton, C. E. Cooper, and R. G. Knowles, Nitric oxide synthases: structure, function and inhibition, Biochemical Journal, vol.357, issue.3, pp.593-615, 2001.
DOI : 10.1042/bj3570593

D. S. Bredt and S. H. Snyder, Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme., Proceedings of the National Academy of Sciences, vol.87, issue.2, pp.682-685, 1990.
DOI : 10.1073/pnas.87.2.682

Q. W. Xie, H. J. Cho, J. Calaycay, R. A. Mumford, K. M. Swiderek et al., Cloning and characterization of inducible nitric oxide synthase from mouse macrophages, Science, vol.256, issue.5054, pp.225-228, 1992.
DOI : 10.1126/science.1373522

D. J. Stuehr, STRUCTURE-FUNCTION ASPECTS IN THE NITRIC OXIDE SYNTHASES, Annual Review of Pharmacology and Toxicology, vol.37, issue.1, pp.339-359, 1997.
DOI : 10.1146/annurev.pharmtox.37.1.339

B. R. Crane, A. S. Arvai, D. K. Ghosh, C. Wu, E. D. Getzoff et al., Structure of Nitric Oxide Synthase Oxygenase Dimer with Pterin and Substrate, Science, vol.279, issue.5359, pp.2121-2126, 1998.
DOI : 10.1126/science.279.5359.2121

B. Mayer and B. Hemmens, Biosynthesis and action of nitric oxide in mammalian cells, Trends in Biochemical Sciences, vol.22, issue.12, pp.477-481, 1997.
DOI : 10.1016/S0968-0004(97)01147-X

D. J. Stuehr, Mammalian nitric oxide synthases, Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol.1411, issue.2-3, pp.217-230, 1999.
DOI : 10.1016/S0005-2728(99)00016-X

URL : http://doi.org/10.1016/s0005-2728(99)00016-x

H. Li and T. L. Poulos, Structure?function studies on nitric oxide synthases, Journal of Inorganic Biochemistry, vol.99, issue.1, pp.293-305, 2005.
DOI : 10.1016/j.jinorgbio.2004.10.016

C. C. Wei, Z. Q. Wang, C. Hemann, R. Hille, and D. J. Stuehr, A Tetrahydrobiopterin Radical Forms and then Becomes Reduced during N??-Hydroxyarginine Oxidation by Nitric-oxide Synthase, Journal of Biological Chemistry, vol.278, issue.47, pp.46668-46673, 2003.
DOI : 10.1074/jbc.M307682200

O. W. Griffith and D. J. Stuehr, Nitric Oxide Synthases: Properties and Catalytic Mechanism, Annual Review of Physiology, vol.57, issue.1, pp.707-736, 1995.
DOI : 10.1146/annurev.ph.57.030195.003423

M. A. Marletta, Nitric oxide synthase: Aspects concerning structure and catalysis, Cell, vol.78, issue.6, pp.927-930, 1994.
DOI : 10.1016/0092-8674(94)90268-2

C. C. Wei, B. R. Crane, and D. J. Stuehr, Tetrahydrobiopterin Radical Enzymology, Chemical Reviews, vol.103, issue.6, pp.2365-2383, 2003.
DOI : 10.1021/cr0204350

H. M. Abu-soud, R. Gachhui, F. M. Raushel, and D. J. Stuehr, The Ferrous-dioxy Complex of Neuronal Nitric Oxide Synthase: DIVERGENT EFFECTS OF L-ARGININE AND TETRAHYDROBIOPTERIN ON ITS STABILITY, Journal of Biological Chemistry, vol.272, issue.28, pp.17349-17353, 1997.
DOI : 10.1074/jbc.272.28.17349

N. C. Gerber, C. R. Nishida, and P. R. Ortiz-de-montellano, Characterization of Human Liver Inducible Nitric Oxide Synthase Expressed inEscherichia coli, Archives of Biochemistry and Biophysics, vol.343, issue.2, pp.249-253, 1997.
DOI : 10.1006/abbi.1997.0187

H. M. Abu-soud, M. Loftus, and D. J. Stuehr, Subunit Dissociation and Unfolding of Macrophage NO Synthase: Relationship between Enzyme Structure, Prosthetic Group Binding, and Catalytic Function, Biochemistry, vol.34, issue.35, pp.11167-11175, 1995.
DOI : 10.1021/bi00035a023

P. P. Schmidt, R. Lange, A. C. Gorren, E. R. Werner, B. Mayer et al., Formation of a protonated trihydrobiopterin radical cation in the first reaction cycle of neuronal and endothelial nitric oxide synthase detected by electron paramagnetic resonance spectroscopy, JBIC Journal of Biological Inorganic Chemistry, vol.6, issue.2, pp.151-158, 2001.
DOI : 10.1007/s007750000185

T. Nagatsu and H. Ichinose, Regulation of pteridine-requiring enzymes by the cofactor tetrahydrobiopterin, Molecular Neurobiology, vol.12, issue.1, pp.79-96, 1999.
DOI : 10.1007/BF02741379

C. S. Raman, H. Li, P. Martasek, V. Kral, B. S. Masters et al., Crystal Structure of Constitutive Endothelial Nitric Oxide Synthase, Cell, vol.95, issue.7, pp.939-950, 1998.
DOI : 10.1016/S0092-8674(00)81718-3

Z. Q. Wang, C. C. Wei, and D. J. Stuehr, A Conserved Tryptophan 457 Modulates the Kinetics and Extent of N-Hydroxy-L-Arginine Oxidation by Inducible Nitric-oxide Synthase, Journal of Biological Chemistry, vol.277, issue.15, pp.12830-12837, 2002.
DOI : 10.1074/jbc.M111967200

I. Sagami, Y. Sato, S. Daff, and T. Shimizu, Aromatic Residues and Neighboring Arg414 in the (6R)-5,6,7,8-Tetrahydro-L-Biopterin Binding Site of Full-length Neuronal Nitric-oxide Synthase Are Crucial in Catalysis and Heme Reduction with NADPH, Journal of Biological Chemistry, vol.275, issue.34, pp.26150-26157, 2000.
DOI : 10.1074/jbc.M000534200

P. F. Chen, V. Berka, and K. K. Wu, Differential effects of mutations in human endothelial nitric oxide synthase at residues Tyr-357 and Arg-365 on l-arginine hydroxylation and GN-hydroxy-l-arginine oxidation, Archives of Biochemistry and Biophysics, vol.411, issue.1, pp.83-92, 2003.
DOI : 10.1016/S0003-9861(02)00729-4

R. A. Pufahl, J. S. Wishnok, and M. A. Marletta, Hydrogen Peroxide-Supported Oxidation of NG-Hydroxy-L-Arginine by Nitric Oxide Synthase, Biochemistry, vol.34, issue.6, pp.1930-1941, 1995.
DOI : 10.1021/bi00006a014

A. Presta, A. M. Weber-main, M. T. Stankovich, and D. J. Stuehr, Comparative Effects of Substrates and Pterin Cofactor on the Heme Midpoint Potential in Inducible and Neuronal Nitric Oxide Synthases, Journal of the American Chemical Society, vol.120, issue.37, pp.9460-9465, 1998.
DOI : 10.1021/ja9740374

J. Tejero, J. Santolini, and D. J. Stuehr, Fast ferrous heme-NO oxidation in nitric oxide synthases, FEBS Journal, vol.274, issue.16, pp.4505-4514, 2009.
DOI : 10.1111/j.1742-4658.2009.07157.x

URL : https://hal.archives-ouvertes.fr/cea-01234308

S. Adak, K. S. Aulak, and D. J. Stuehr, Chimeras of Nitric-oxide Synthase Types I and III Establish Fundamental Correlates between Heme Reduction, Heme-NO Complex Formation, and Catalytic Activity, Journal of Biological Chemistry, vol.276, issue.26, pp.23246-23252, 2001.
DOI : 10.1074/jbc.M102509200

S. Adak, Q. Wang, and D. J. Stuehr, Molecular Basis for Hyperactivity in Tryptophan 409 Mutants of Neuronal NO Synthase, Journal of Biological Chemistry, vol.275, issue.23, pp.17434-17439, 2000.
DOI : 10.1074/jbc.M000846200

J. Santolini, A. L. Meade, and D. J. Stuehr, Differences in Three Kinetic Parameters Underpin the Unique Catalytic Profiles of Nitric-oxide Synthases I, II, and III, Journal of Biological Chemistry, vol.276, issue.52, pp.48887-48898, 2001.
DOI : 10.1074/jbc.M108666200

Z. Q. Wang, C. C. Wei, and D. J. Stuehr, How does a valine residue that modulates heme-NO binding kinetics in inducible NO synthase regulate enzyme catalysis?, Journal of Inorganic Biochemistry, vol.104, issue.3, pp.349-356, 2010.
DOI : 10.1016/j.jinorgbio.2009.11.006

S. Adak, Q. Wang, and D. J. Stuehr, Arginine Conversion to Nitroxide by Tetrahydrobiopterin-free Neuronal Nitric-oxide Synthase: IMPLICATIONS FOR MECHANISM, Journal of Biological Chemistry, vol.275, issue.43, pp.33554-33561, 2000.
DOI : 10.1074/jbc.M004337200

S. Adak and D. J. Stuehr, A proximal tryptophan in NO synthase controls activity by a novel mechanism, Journal of Inorganic Biochemistry, vol.83, issue.4, pp.301-308, 2001.
DOI : 10.1016/S0162-0134(00)00176-8

T. W. Ost and S. Daff, Thermodynamic and Kinetic Analysis of the Nitrosyl, Carbonyl, and Dioxy Heme Complexes of Neuronal Nitric-oxide Synthase: THE ROLES OF SUBSTRATE AND TETRAHYDROBIOPTERIN IN OXYGEN ACTIVATION, Journal of Biological Chemistry, vol.280, issue.2, pp.965-973, 2005.
DOI : 10.1074/jbc.M411191200

C. E. Cooper, Nitric oxide and iron proteins, Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol.1411, issue.2-3, pp.290-309, 1999.
DOI : 10.1016/S0005-2728(99)00021-3

D. J. Stuehr, J. Santolini, Z. Q. Wang, C. C. Wei, and S. Adak, Update on Mechanism and Catalytic Regulation in the NO Synthases, Journal of Biological Chemistry, vol.279, issue.35, pp.36167-36170, 2004.
DOI : 10.1074/jbc.R400017200

N. Bec, A. C. Gorren, C. Voelker, B. Mayer, and R. Lange, Reaction of Neuronal Nitric-oxide Synthase with Oxygen at Low Temperature: EVIDENCE FOR REDUCTIVE ACTIVATION OF THE OXY-FERROUS COMPLEX BY TETRAHYDROBIOPTERIN, Journal of Biological Chemistry, vol.273, issue.22, pp.13502-13508, 1998.
DOI : 10.1074/jbc.273.22.13502

M. A. Marletta, A. R. Hurshman, and K. M. Rusche, Catalysis by nitric oxide synthase, Current Opinion in Chemical Biology, vol.2, issue.5, pp.656-663, 1998.
DOI : 10.1016/S1367-5931(98)80098-7

B. R. Crane, A. S. Arvai, R. Gachhui, C. Wu, D. K. Ghosh et al., The Structure of Nitric Oxide Synthase Oxygenase Domain and Inhibitor Complexes, Science, vol.278, issue.5337, pp.425-431, 1997.
DOI : 10.1126/science.278.5337.425