메뉴 건너뛰기




Volumn , Issue 21, 2005, Pages 3427-3435

Exploring the redox reactions between heme and tetrahydrobiopterin in the nitric oxide synthases

Author keywords

[No Author keywords available]

Indexed keywords

NITRIC OXIDE (NO); NO SYNTHASES (NOS); REDOX TRANSITION; TETRAHYDROBIOPERTIN;

EID: 27744480772     PISSN: 14779226     EISSN: 14779234     Source Type: Journal    
DOI: 10.1039/b506355h     Document Type: Review
Times cited : (45)

References (86)
  • 1
    • 0019463506 scopus 로고
    • Nitrate synthesis and reduction in the germ-free and conventional rat
    • L. C. Green, S. R. Tannenbaum and P. Goldman, Nitrate synthesis and reduction in the germ-free and conventional rat, Science, 1981, 212, 56-58.
    • (1981) Science , vol.212 , pp. 56-58
    • Green, L.C.1    Tannenbaum, S.R.2    Goldman, P.3
  • 2
    • 0024549389 scopus 로고
    • Activated murine macrophages secrete a metabolite of arginine with the bioactivity of endothelium-derived relaxing factor and the chemical reactivity of nitric oxide
    • D. J. Stuehr, S. S. Gross, I. Sakuma, R. Levi and C. F. Nathan, Activated murine macrophages secrete a metabolite of arginine with the bioactivity of endothelium-derived relaxing factor and the chemical reactivity of nitric oxide, J. Exp. Med., 1989, 169, 1011-1020.
    • (1989) J. Exp. Med. , vol.169 , pp. 1011-1020
    • Stuehr, D.J.1    Gross, S.S.2    Sakuma, I.3    Levi, R.4    Nathan, C.F.5
  • 4
    • 0023198721 scopus 로고
    • Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor
    • R. M.-J. Palmer, A. G. Ferrige and S. Moncada, Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor, Nature, 1987, 327, 524-526.
    • (1987) Nature , vol.327 , pp. 524-526
    • Palmer, R.M.-J.1    Ferrige, A.G.2    Moncada, S.3
  • 5
    • 0023505509 scopus 로고
    • Endothelium-derived relaxing factor produced and released from artery and vein is nitric oxide
    • L. J. Ignarro, G. M. Buga, K. S. Wood, R. E. Byrns and G. Chaudhuri, Endothelium-derived relaxing factor produced and released from artery and vein is nitric oxide, Proc. Natl. Acad. Sci. USA, 1987, 84, 9265-9269.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 9265-9269
    • Ignarro, L.J.1    Buga, G.M.2    Wood, K.S.3    Byrns, R.E.4    Chaudhuri, G.5
  • 6
    • 0028128416 scopus 로고
    • NO at work
    • H. H. W. Schmidt and U. Walter, NO at work, Cell, 1994, 78, 919-925.
    • (1994) Cell , vol.78 , pp. 919-925
    • Schmidt, H.H.W.1    Walter, U.2
  • 7
    • 0028902552 scopus 로고
    • Nitric oxide synthases: Properties and catalytic mechanism
    • O. W. Griffith and D. J. Stuehr, Nitric Oxide Synthases: Properties and Catalytic Mechanism, Annu. Rev. Physiol., 1995, 57, 707-736.
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 707-736
    • Griffith, O.W.1    Stuehr, D.J.2
  • 8
    • 0027975453 scopus 로고
    • Nitric Oxide: A physiologic messenger molecule
    • D. S. Bredt and S. H. Snyder, Nitric Oxide: A physiologic messenger molecule, Annu. Rev. Biochem., 1994, 63, 175-195.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 175-195
    • Bredt, D.S.1    Snyder, S.H.2
  • 9
    • 0001226142 scopus 로고
    • Nitric oxide in cells
    • J. R. Lancaster, Jr., Nitric oxide in cells, Sci. Am., 1992, 80, 248-259.
    • (1992) Sci. Am. , vol.80 , pp. 248-259
    • Lancaster Jr., J.R.1
  • 10
    • 77954970807 scopus 로고
    • Diffusable messengers and intercellular signaling: Locally distributed synaptic potentiation in the hippocampus
    • D. V. Madison and E. M. Schuman, Diffusable messengers and intercellular signaling: Locally distributed synaptic potentiation in the hippocampus, Curr. Top. Microbiol. Immunol., 1993, 19605-19610.
    • (1993) Curr. Top. Microbiol. Immunol. , pp. 19605-19610
    • Madison, D.V.1    Schuman, E.M.2
  • 11
    • 0026077959 scopus 로고
    • Glutamate, nitric oxide and cell-cell signalling in the nervous system
    • J. Garthwaite, Glutamate, nitric oxide and cell-cell signalling in the nervous system, Trends Neurosci., 1991, 14, 60-67.
    • (1991) Trends Neurosci. , vol.14 , pp. 60-67
    • Garthwaite, J.1
  • 13
    • 0035929149 scopus 로고    scopus 로고
    • Nitrosylation. the prototypic redox-based signaling mechanism
    • J. S. Stamler, S. Lamas and F. C. Fang, Nitrosylation. The prototypic redox-based signaling mechanism, Cell, 2001, 106, 675-683.
    • (2001) Cell , vol.106 , pp. 675-683
    • Stamler, J.S.1    Lamas, S.2    Fang, F.C.3
  • 14
    • 0035846988 scopus 로고    scopus 로고
    • A kinetic simulation model that describes catalysis and regulation in nitric-oxide synthase
    • J. Santolini, S. Adak, C. M. Curran and D. J. Stuehr, A kinetic simulation model that describes catalysis and regulation in nitric-oxide synthase, J. Biol. Chem., 2001, 276, 1233-1243.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1233-1243
    • Santolini, J.1    Adak, S.2    Curran, C.M.3    Stuehr, D.J.4
  • 15
    • 0035966114 scopus 로고    scopus 로고
    • Differences in three kinetic parameters underpin the unique catalytic profiles of nitric-oxide synthases I, II, and III
    • 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, J. Biol. Chem., 2001, 276, 48887-48898.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48887-48898
    • Santolini, J.1    Meade, A.L.2    Stuehr, D.J.3
  • 16
    • 0034681455 scopus 로고    scopus 로고
    • Endothelial nitric-oxide synthase (type III) is activated and becomes calcium independent upon phosphorylation by cyclic nucleotide-dependent protein kinases
    • E. Butt, M. Bernhardt, A. Smolenski, P. Kotsonis, L. G. Frohlich, A. Sickmann, H. E. Meyer, S. M. Lohmann and H. H. Schmidt, Endothelial nitric-oxide synthase (type III) is activated and becomes calcium independent upon phosphorylation by cyclic nucleotide-dependent protein kinases, J. Biol Chem., 2000, 275, 5179-5187.
    • (2000) J. Biol Chem. , vol.275 , pp. 5179-5187
    • Butt, E.1    Bernhardt, M.2    Smolenski, A.3    Kotsonis, P.4    Frohlich, L.G.5    Sickmann, A.6    Meyer, H.E.7    Lohmann, S.M.8    Schmidt, H.H.9
  • 17
    • 0035844241 scopus 로고    scopus 로고
    • Reciprocal phosphorylation and regulation of endothelial nitric-oxide synthase in response to bradykinin stimulation
    • M. B. Harris, H. Ju, V. J. Venema, H. Liang, R. Zou, B. J. Michell, Z. P. Chen, B. E. Kemp and R. C. Venema, Reciprocal phosphorylation and regulation of endothelial nitric-oxide synthase in response to bradykinin stimulation, J. Biol. Chem., 2001, 276, 16587-16591.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16587-16591
    • Harris, M.B.1    Ju, H.2    Venema, V.J.3    Liang, H.4    Zou, R.5    Michell, B.J.6    Chen, Z.P.7    Kemp, B.E.8    Venema, R.C.9
  • 18
    • 0035902480 scopus 로고    scopus 로고
    • Complex regulation of human inducible nitric oxide synthase gene transcription by Stat 1 and NF-kappa B
    • R. W. Ganster, B. S. Taylor, L. Shao and D. A. Geller, Complex regulation of human inducible nitric oxide synthase gene transcription by Stat 1 and NF-kappa B, Proc. Natl. Acad. Sci. USA, 2001, 98, 8638-8643.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8638-8643
    • Ganster, R.W.1    Taylor, B.S.2    Shao, L.3    Geller, D.A.4
  • 20
    • 0035449121 scopus 로고    scopus 로고
    • Another activation switch for endothelial nitric oxide synthase: Why does it have to be so complicated?
    • M. A. Marletta, Another activation switch for endothelial nitric oxide synthase: why does it have to be so complicated?, Trends Biochem. Sci., 2001, 26, 519-521.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 519-521
    • Marletta, M.A.1
  • 21
    • 0029966119 scopus 로고    scopus 로고
    • Neuronal nitric oxide synthase, a modular enzyme formed by convergent evolution: Structure studies of a cysteine thiolate-liganded heme protein that hydroxylates L-arginine to produce NO as a cellular signal
    • B. S. S. Masters, K. McMillan, E. A. Sheta, J. S. Nishimura, L. J. Roman and P. Martasek, Neuronal nitric oxide synthase, a modular enzyme formed by convergent evolution: Structure studies of a cysteine thiolate-liganded heme protein that hydroxylates L-arginine to produce NO as a cellular signal, FASEB J., 1996, 10, 552-558.
    • (1996) FASEB J. , vol.10 , pp. 552-558
    • Masters, B.S.S.1    McMillan, K.2    Sheta, E.A.3    Nishimura, J.S.4    Roman, L.J.5    Martasek, P.6
  • 23
    • 0029983264 scopus 로고    scopus 로고
    • Identification, characterization, and comparison of the calmodulin-binding domain of the endothelial and inducible, nitric oxide synthases
    • R. C. Venema, H. S. Sayegh, J. D. Kent and D. G. Harrison, Identification, characterization, and comparison of the calmodulin-binding domain of the endothelial and inducible, nitric oxide synthases, J. Biol. Chem., 1996, 271, 6435-6440.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6435-6440
    • Venema, R.C.1    Sayegh, H.S.2    Kent, J.D.3    Harrison, D.G.4
  • 24
    • 0030988217 scopus 로고    scopus 로고
    • Structure-function aspects in the nitric oxide synthases
    • D. J. Stuehr, Structure-function aspects in the nitric oxide synthases, Annu. Rev. Pharmacol. Toxicol., 1997, 37, 339-359.
    • (1997) Annu. Rev. Pharmacol. Toxicol. , vol.37 , pp. 339-359
    • Stuehr, D.J.1
  • 25
    • 0028026868 scopus 로고
    • Nitric oxide synthase: Aspects concerning structure and catalysis
    • M. A. Marietta, Nitric oxide synthase: Aspects concerning structure and catalysis, Cell, 1994, 78, 927-930.
    • (1994) Cell , vol.78 , pp. 927-930
    • Marietta, M.A.1
  • 26
    • 0028582164 scopus 로고
    • Calmodulin controls neuronal nitric-oxide synthase by a dual mechanism. Activation of intra- And interdomain electron transfer
    • H. M. Abu-Soud, L. L. Yoho and D. J. Stuehr, Calmodulin controls neuronal nitric-oxide synthase by a dual mechanism. Activation of intra- and interdomain electron transfer, J. Biol. Chem., 1994, 269, 32047-32050.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32047-32050
    • Abu-Soud, H.M.1    Yoho, L.L.2    Stuehr, D.J.3
  • 27
    • 0032732706 scopus 로고    scopus 로고
    • Calmodulin activates intramolecular electron transfer between the two flavins of neuronal nitric oxide synthase flavin domain
    • H. Matsuda and T. Iyanagi, Calmodulin activates intramolecular electron transfer between the two flavins of neuronal nitric oxide synthase flavin domain, Biochim. Biophys. Acta, 1999, 1473, 345-355.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 345-355
    • Matsuda, H.1    Iyanagi, T.2
  • 28
    • 0039000253 scopus 로고    scopus 로고
    • The C terminus of mouse macrophage inducible nitric-oxide synthase attenuates electron flow through the flavin domain
    • L. J. Roman, R. T. Miller, M. A. de La Garza, J. J. Kim and B. S. S. Siler Masters, The C terminus of mouse macrophage inducible nitric-oxide synthase attenuates electron flow through the flavin domain, J. Biol. Chem., 2000, 275, 21914-21919.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21914-21919
    • Roman, L.J.1    Miller, R.T.2    De La Garza, M.A.3    Kim, J.J.4    Siler Masters, B.S.S.5
  • 29
    • 0035947583 scopus 로고    scopus 로고
    • Heat shock protein 90 mediates the balance of nitric oxide and Superoxide anion from endothelial nitric-oxide synthase
    • K. A. Pritchard, Jr., A. W. Ackerman, E. R. Gross, D. W. Stepp, Y. Shi, J. T. Fontana, J. E. Baker and W. C. Sessa, Heat shock protein 90 mediates the balance of nitric oxide and Superoxide anion from endothelial nitric-oxide synthase, J. Biol Chem., 2001, 276, 17621-17624.
    • (2001) J. Biol Chem. , vol.276 , pp. 17621-17624
    • Pritchard Jr., K.A.1    Ackerman, A.W.2    Gross, E.R.3    Stepp, D.W.4    Shi, Y.5    Fontana, J.T.6    Baker, J.E.7    Sessa, W.C.8
  • 31
  • 32
    • 0032416666 scopus 로고    scopus 로고
    • Crystal structure of constitutive endothelial nitric oxide synthase: A paradigm for pterin function involving a novel metal center
    • C. S. Raman, H. Li, P. Martasek, V. Krai, B. S. Masters and T. L. Poulos, Crystal structure of constitutive endothelial nitric oxide synthase: a paradigm for pterin function involving a novel metal center, Cell, 1998, 95, 939-950.
    • (1998) Cell , vol.95 , pp. 939-950
    • Raman, C.S.1    Li, H.2    Martasek, P.3    Krai, V.4    Masters, B.S.5    Poulos, T.L.6
  • 35
    • 0025976756 scopus 로고
    • An unusual yet strongly conserved flavoprotein reductase in bacteriaand mammals
    • T. D. Porter, An unusual yet strongly conserved flavoprotein reductase in bacteriaand mammals, Trends Biochem. Sci., 1991, 16, 154-158.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 154-158
    • Porter, T.D.1
  • 36
    • 0035813091 scopus 로고    scopus 로고
    • Crystal structure of the FAD/NADPH binding domain of rat neuronal NO synthase: Comparisons with NADPH cytochrome P450 oxidoreductase
    • J. Zhang, P. Martasek, R. Paschke, T. Shea, B. S. S. Masters and J. J. Kim, Crystal structure of the FAD/NADPH binding domain of rat neuronal NO synthase: Comparisons with NADPH cytochrome P450 oxidoreductase, J. Biol. Chem., 2001, 276, 37506-37513.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37506-37513
    • Zhang, J.1    Martasek, P.2    Paschke, R.3    Shea, T.4    Masters, B.S.S.5    Kim, J.J.6
  • 37
    • 0030007024 scopus 로고    scopus 로고
    • Endothelial nitric-oxide synthase. Evidence for bidomain structure and successful reconstitution of catalytic activity from two separate domains generated by a baculovirus expression system
    • P. F. Chen, A. L. Tsai, V. Berka and K. K. Wu, Endothelial nitric-oxide synthase. Evidence for bidomain structure and successful reconstitution of catalytic activity from two separate domains generated by a baculovirus expression system, J. Biol. Chem., 1996, 271, 14631-14635.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14631-14635
    • Chen, P.F.1    Tsai, A.L.2    Berka, V.3    Wu, K.K.4
  • 38
    • 0028931726 scopus 로고
    • Prokaryotic expression of the heme-and flavin-binding domains of rat neuronal nitric oxide synthase as distinct polypeptides: Identification of the heme-binding proximal thiolate ligand as cysteine-415
    • K. McMillan and B. S. Masters, Prokaryotic expression of the heme-and flavin-binding domains of rat neuronal nitric oxide synthase as distinct polypeptides: identification of the heme-binding proximal thiolate ligand as cysteine-415, Biochemistry, 1995, 34, 3686-3693.
    • (1995) Biochemistry , vol.34 , pp. 3686-3693
    • McMillan, K.1    Masters, B.S.2
  • 39
    • 0024388901 scopus 로고
    • Macrophage oxidation of L-arginine to nitric oxide, nitrite, and nitrate. Tetrahydrobiopterin is required as a cofactor
    • M. A. Tayeh and M. A. Marletta, Macrophage oxidation of L-arginine to nitric oxide, nitrite, and nitrate. Tetrahydrobiopterin is required as a cofactor, J. Biol. Chem., 1989, 264, 19654-19658.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19654-19658
    • Tayeh, M.A.1    Marletta, M.A.2
  • 40
    • 0024351625 scopus 로고
    • Reduced biopterin as a cofactor in the generation of nitrogen oxides by murine macrophages
    • N. S. Kwon, C. F. Nathan and D. J. Stuehr, Reduced biopterin as a cofactor in the generation of nitrogen oxides by murine macrophages, J. Biol. Chem., 1989, 264, 20496-20501.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20496-20501
    • Kwon, N.S.1    Nathan, C.F.2    Stuehr, D.J.3
  • 41
    • 0025572626 scopus 로고
    • Purification of a Ca2+/calmodulin-dependent nitric oxide synthase from porcine cerebellum. Cofactor-role of tetrahydrobiopterin
    • B. Mayer, M. John and E. Bohme, Purification of a Ca2+/calmodulin- dependent nitric oxide synthase from porcine cerebellum. Cofactor-role of tetrahydrobiopterin, FEBS Lett., 1990, 277, 215-219.
    • (1990) FEBS Lett. , vol.277 , pp. 215-219
    • Mayer, B.1    John, M.2    Bohme, E.3
  • 42
    • 0032852842 scopus 로고    scopus 로고
    • Tetrahydropterin-dependent amino acid hydroxy-lases
    • P. F. Fitzpatrick, Tetrahydropterin-dependent amino acid hydroxy-lases., Annu. Rev. Biochem., 1999, 68, 355-381.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 355-381
    • Fitzpatrick, P.F.1
  • 44
    • 0028902552 scopus 로고
    • Nitric oxide synthases: Properties and catalytic mechanism
    • W. Griffith and D. J. Stuehr, Nitric oxide synthases: properties and catalytic mechanism, Annu. Rev. Physiol., 1995, 57, 707-736.
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 707-736
    • Griffith, W.1    Stuehr, D.J.2
  • 45
    • 0029121435 scopus 로고
    • Identification of nitric oxide synthase as a thiolate-ligated heme protein using magnetic circular dichroism spectroscopy. Comparison with cytochrome P-450-CAM andchloroperoxidase
    • M. Sono, D. J. Stuehr, M. Ikeda-Saito and J. H. Dawson, Identification of nitric oxide synthase as a thiolate-ligated heme protein using magnetic circular dichroism spectroscopy. Comparison with cytochrome P-450-CAM andchloroperoxidase, J. Biol. Chem., 1995, 270, 19943-19948.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19943-19948
    • Sono, M.1    Stuehr, D.J.2    Ikeda-Saito, M.3    Dawson, J.H.4
  • 46
    • 0030859931 scopus 로고    scopus 로고
    • The ferrous-dioxy complex of neuronal nitric oxide synthase. Divergent effects of L-arginine and tetrahydrobiopterin on its stability
    • 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, J. Biol. Chem., 1997, 272, 17349-17353.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17349-17353
    • Abu-Soud, H.M.1    Gachhui, R.2    Raushel, F.M.3    Stuehr, D.J.4
  • 47
    • 0034718572 scopus 로고    scopus 로고
    • Low-temperature optical absorption spectra suggest a redox role for tetrahydrobiopterin in both steps of nitric oxide synthase catalysis
    • A. C. Gorren, N. Bee, A. Schrammel, E. R. Werner, R. Lange and B. Mayer, Low-temperature optical absorption spectra suggest a redox role for tetrahydrobiopterin in both steps of nitric oxide synthase catalysis, Biochemistry, 2000, 39, 11763-11770.
    • (2000) Biochemistry , vol.39 , pp. 11763-11770
    • Gorren, A.C.1    Bee, N.2    Schrammel, A.3    Werner, E.R.4    Lange, R.5    Mayer, B.6
  • 48
    • 0034603038 scopus 로고    scopus 로고
    • The ferrous dioxygen complex of the oxygenase domain of neuronal nitric-oxide synthase
    • M. Couture, D. J. Stuehr and D. L. Rousseau, The ferrous dioxygen complex of the oxygenase domain of neuronal nitric-oxide synthase, J. Biol. Chem., 2000, 275, 3201-3205.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3201-3205
    • Couture, M.1    Stuehr, D.J.2    Rousseau, D.L.3
  • 49
    • 0032583467 scopus 로고    scopus 로고
    • Autoxidation rates of neuronal nitric oxide synthase: Effects of the substrates, inhibitors, and modulators
    • H. Sato, I. Sagami, S. Daff and T. Shimizu, Autoxidation rates of neuronal nitric oxide synthase: effects of the substrates, inhibitors, and modulators, Biochem. Biophys. Res. Commun., 1998, 253, 845-849.
    • (1998) Biochem. Biophys. Res. Commun. , vol.253 , pp. 845-849
    • Sato, H.1    Sagami, I.2    Daff, S.3    Shimizu, T.4
  • 50
    • 0033594933 scopus 로고    scopus 로고
    • Low-temperature stabilization and spectroscopic characterization of the dioxygen complex of the ferrous neuronal nitric oxide synthase oxygenase domain
    • A. P. Ledbetter, K. McMillan, L. J. Roman, B. S. S. Masters, J. H. Dawson and M. Sono, Low-temperature stabilization and spectroscopic characterization of the dioxygen complex of the ferrous neuronal nitric oxide synthase oxygenase domain, Biochemistry, 1999, 38, 8014-8021.
    • (1999) Biochemistry , vol.38 , pp. 8014-8021
    • Ledbetter, A.P.1    McMillan, K.2    Roman, L.J.3    Masters, B.S.S.4    Dawson, J.H.5    Sono, M.6
  • 51
    • 0032416666 scopus 로고    scopus 로고
    • Crystal structure of constitutive endothelial nitric oxide synthase: A paradigm for pterin function involving a novel metal center
    • C. S. Raman, H. Li, P. Martasek, V. Kral, B. B. S. Masters and T. M. Poulos, Crystal structure of constitutive endothelial nitric oxide synthase: a paradigm for pterin function involving a novel metal center, Cell, 1998, 95, 939-950.
    • (1998) Cell , vol.95 , pp. 939-950
    • Raman, C.S.1    Li, H.2    Martasek, P.3    Kral, V.4    Masters, B.B.S.5    Poulos, T.M.6
  • 52
    • 0032577582 scopus 로고    scopus 로고
    • Reaction of neuronal nitric-oxide synthase with oxygen at low temperature. Evidence for reductive activation of the oxy-ferrous complex by tetrahydrobiopterin
    • N. Bee, 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, J. Biol. Chem., 1998, 273, 13502-13508.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13502-13508
    • Bee, N.1    Gorren, A.C.2    Voelker, C.3    Mayer, B.4    Lange, R.5
  • 53
    • 0034721839 scopus 로고    scopus 로고
    • Arginine conversion tonitroxide by tetrahydrobiopterin-free neuronal nitric-oxide synthase. Implications for mechanism
    • S. Adak, Q. Wang and D. J. Stuehr, Arginine conversion tonitroxide by tetrahydrobiopterin-free neuronal nitric-oxide synthase. Implications for mechanism, J. Biol. Chem., 2000, 275, 33554-33561.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33554-33561
    • Adak, S.1    Wang, Q.2    Stuehr, D.J.3
  • 54
    • 0030464496 scopus 로고    scopus 로고
    • Tetrahydrobiopterin-free neuronal nitric oxide synthase: Evidence for two identical highly anticooperative pteridine binding sites
    • A. C. Gorren, B. M. List, A. Schrammel, E. Pitters, B. Hemmens, E. R. Werner, K. Schmidt and B. Mayer, Tetrahydrobiopterin-free neuronal nitric oxide synthase: evidence for two identical highly anticooperative pteridine binding sites, Biochemistry, 1996, 35, 16735-16745.
    • (1996) Biochemistry , vol.35 , pp. 16735-16745
    • Gorren, A.C.1    List, B.M.2    Schrammel, A.3    Pitters, E.4    Hemmens, B.5    Werner, E.R.6    Schmidt, K.7    Mayer, B.8
  • 55
    • 1542548514 scopus 로고    scopus 로고
    • Single-turnover of nitric-oxide synthase in the presence of 4-amino-tetrahydrobiopterin: Proposed role for tetrahydrobiopterin as a proton donor
    • M. Sorlie, A. C. Gorren, S. Marchal, T. Shimizu, R. Lange, K. K. Andersson and B. Mayer, Single-turnover of nitric-oxide synthase in the presence of 4-amino-tetrahydrobiopterin: proposed role for tetrahydrobiopterin as a proton donor, J. Biol. Chem., 2003, 278, 48602-48610.
    • (2003) J. Biol. Chem. , vol.278 , pp. 48602-48610
    • Sorlie, M.1    Gorren, A.C.2    Marchal, S.3    Shimizu, T.4    Lange, R.5    Andersson, K.K.6    Mayer, B.7
  • 56
    • 0033570117 scopus 로고    scopus 로고
    • Reactivity of tetrahydrobiopterin bound to nitric-oxide synthase
    • C. F. B. Witteveen, J. Giovanelli and S. Kaufman, Reactivity of tetrahydrobiopterin bound to nitric-oxide synthase, J. Biol. Chem., 1999, 274, 29755-29762.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29755-29762
    • Witteveen, C.F.B.1    Giovanelli, J.2    Kaufman, S.3
  • 58
    • 0033619713 scopus 로고    scopus 로고
    • Formation of a pterin radical in the reaction of the heme domain of inducible nitric oxide synthase with oxygen
    • A. R. Hurshman, C. Krebs, D. E. Edmondson, B. H. Huynh and M. A. Marietta, Formation of a pterin radical in the reaction of the heme domain of inducible nitric oxide synthase with oxygen, Biochemistry, 1999, 38, 15689-15696.
    • (1999) Biochemistry , vol.38 , pp. 15689-15696
    • Hurshman, A.R.1    Krebs, C.2    Edmondson, D.E.3    Huynh, B.H.4    Marietta, M.A.5
  • 59
    • 0034852561 scopus 로고    scopus 로고
    • 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
    • P. P. Schmidt, R. Lange, A. C. Gorren, E. R. Werner, B. Mayer and K. K. Andersson, 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, J. Biol. Inorg. Chem., 2001, 6, 151-158.
    • (2001) J. Biol. Inorg. Chem. , vol.6 , pp. 151-158
    • Schmidt, P.P.1    Lange, R.2    Gorren, A.C.3    Werner, E.R.4    Mayer, B.5    Andersson, K.K.6
  • 60
    • 0034105813 scopus 로고    scopus 로고
    • Formation and reactions of the heme-dioxygen intermediate in the first and second steps of nitric oxide synthesis as studied by stopped-flow spectroscopy under single-turnover conditions
    • S. Boggs, L. Huang and D. J. Stuehr, Formation and reactions of the heme-dioxygen intermediate in the first and second steps of nitric oxide synthesis as studied by stopped-flow spectroscopy under single-turnover conditions, Biochemistry, 2000, 39, 2332-2339.
    • (2000) Biochemistry , vol.39 , pp. 2332-2339
    • Boggs, S.1    Huang, L.2    Stuehr, D.J.3
  • 61
    • 0033554859 scopus 로고    scopus 로고
    • Kinetic studies on the successive reaction of neuronal nitric oxide synthase from L-arginine to nitric oxide and L-citrulline
    • T. Iwanaga, T. Yamazaki and S. Kominami, Kinetic studies on the successive reaction of neuronal nitric oxide synthase from L-arginine to nitric oxide and L-citrulline, Biochemistry, 1999, 38, 16629-16635.
    • (1999) Biochemistry , vol.38 , pp. 16629-16635
    • Iwanaga, T.1    Yamazaki, T.2    Kominami, S.3
  • 62
    • 0035808315 scopus 로고    scopus 로고
    • Rapid kinetic studies link tetrahydrobiopterin radical formation to heme-dioxy reduction and arginine hydroxylation in inducible nitric-oxide synthase
    • C.-C. Wei, Z.-Q. Wang, Q. Wang, A. Meade, C. Hemann, R. Hille and D. J. Stuehr, Rapid kinetic studies link tetrahydrobiopterin radical formation to heme-dioxy reduction and arginine hydroxylation in inducible nitric-oxide synthase, J. Biol. Chem., 2001, 276, 315-319.
    • (2001) J. Biol. Chem. , vol.276 , pp. 315-319
    • Wei, C.-C.1    Wang, Z.-Q.2    Wang, Q.3    Meade, A.4    Hemann, C.5    Hille, R.6    Stuehr, D.J.7
  • 64
    • 5444247065 scopus 로고    scopus 로고
    • Redox function of tetrahydrobiopterin and effect of L-arginine on oxygen binding in endothelial nitric oxide synthase
    • V. Berka, H. C. Yeh, D. Gao, F. Kiran and A. L. Tsai, Redox function of tetrahydrobiopterin and effect of L-arginine on oxygen binding in endothelial nitric oxide synthase, Biochemistry, 2004, 43, 13137-48.
    • (2004) Biochemistry , vol.43 , pp. 13137-13148
    • Berka, V.1    Yeh, H.C.2    Gao, D.3    Kiran, F.4    Tsai, A.L.5
  • 65
    • 0033619713 scopus 로고    scopus 로고
    • Formation of a pterin radical' in the reaction of the heme domain of inducible nitric oxide synthase with oxygen
    • A. R. Hurshman, C. Krebs, D. E. Edmondson, B. H. Huynh and M. A. Marletta, Formation of a pterin radical' in the reaction of the heme domain of inducible nitric oxide synthase with oxygen, Biochemistry, 1999, 38, 15689-15696.
    • (1999) Biochemistry , vol.38 , pp. 15689-15696
    • Hurshman, A.R.1    Krebs, C.2    Edmondson, D.E.3    Huynh, B.H.4    Marletta, M.A.5
  • 66
    • 0035980258 scopus 로고    scopus 로고
    • A conserved trytophan in nitric oxide synthesis regulates heme-dioxy reduction by tetrahydrobiopterin
    • Z.-Q. Wang, C.-C. Wei, S. Ghosh, A. L. Meade, C. Hemann, R. Hille and D. J. Stuehr, A Conserved Trytophan In Nitric Oxide Synthesis Regulates Heme-dioxy Reduction by Tetrahydrobiopterin, Biochemistry, 2001, 40, 12819-12825.
    • (2001) Biochemistry , vol.40 , pp. 12819-12825
    • Wang, Z.-Q.1    Wei, C.-C.2    Ghosh, S.3    Meade, A.L.4    Hemann, C.5    Hille, R.6    Stuehr, D.J.7
  • 67
    • 0037066691 scopus 로고    scopus 로고
    • A conserved tryptophan 457 modulates the kinetics and extent of N-hydroxy-L-arginine oxidation by inducible nitric oxide synthase
    • 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, J. Biol. Chem., 2002, 277, 12830-7.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12830-12837
    • Wang, Z.-Q.1    Wei, C.-C.2    Stuehr, D.J.3
  • 68
    • 2442498473 scopus 로고    scopus 로고
    • A conserved Val to He switch near the heme pocket of animal and bacterial nitric-oxide synthases helps determine their distinct catalytic profiles
    • Z.-Q. Wang, C.-C. Wei, M. Sharma, K. Pant, B. R. Crane and D. J. Stuehr, A conserved Val to He switch near the heme pocket of animal and bacterial nitric-oxide synthases helps determine their distinct catalytic profiles, J. Biol. Chem., 2004, 279, 19018-19025.
    • (2004) J. Biol. Chem. , vol.279 , pp. 19018-19025
    • Wang, Z.-Q.1    Wei, C.-C.2    Sharma, M.3    Pant, K.4    Crane, B.R.5    Stuehr, D.J.6
  • 69
    • 15744396356 scopus 로고    scopus 로고
    • The three nitric oxide synthases differ in their kinetics of tetrahydrobiopterin radical formation, heme-dioxy reduction, and arginine hydroxylation
    • C.-C. Wei, Z.-Q. Wang, D. Durra, C. Hemann, R. Hille, E. Garcin, E. D. Getzoff and D. J. Stuehr, The three nitric oxide synthases differ in their kinetics of tetrahydrobiopterin radical formation, heme-dioxy reduction, and arginine hydroxylation, J. Biol. Chem., 2005, 280, 8929-8935.
    • (2005) J. Biol. Chem. , vol.280 , pp. 8929-8935
    • Wei, C.-C.1    Wang, Z.-Q.2    Durra, D.3    Hemann, C.4    Hille, R.5    Garcin, E.6    Getzoff, E.D.7    Stuehr, D.J.8
  • 70
    • 0345306661 scopus 로고    scopus 로고
    • A tetrahydrobiopterin radical forms and then becomes reduced during Nomega-hydroxyarginine oxidation by nitric-oxide synthase
    • C.-C. Wei, Z.-Q. Wang, C. Hemann, R. Hille and D. J. Stuehr, A tetrahydrobiopterin radical forms and then becomes reduced during Nomega-hydroxyarginine oxidation by nitric-oxide synthase, J. Biol. Chem., 2003, 278, 46668-46673.
    • (2003) J. Biol. Chem. , vol.278 , pp. 46668-46673
    • Wei, C.-C.1    Wang, Z.-Q.2    Hemann, C.3    Hille, R.4    Stuehr, D.J.5
  • 71
    • 0037465508 scopus 로고    scopus 로고
    • Structure of tetrahydrobiopterin tunes its electron transfer to the heme-dioxy intermediate in nitric oxide synthase
    • C.-C. Wei, Z.-Q. Wang, A. S. Arvai, C. Hemann, R. Hille, E. D. Getzoff and D. J. Stuehr, Structure of Tetrahydrobiopterin Tunes Its Electron Transfer to the Heme-dioxy Intermediate in Nitric oxide synthase, Biochemistry, 2003, 42, 1969-1977.
    • (2003) Biochemistry , vol.42 , pp. 1969-1977
    • Wei, C.-C.1    Wang, Z.-Q.2    Arvai, A.S.3    Hemann, C.4    Hille, R.5    Getzoff, E.D.6    Stuehr, D.J.7
  • 72
    • 0037898947 scopus 로고    scopus 로고
    • Tetrahydrobiopterin radical enzymology
    • C.-C. Wei, B. R. Crane and D. J. Stuehr, Tetrahydrobiopterin radical enzymology, Chem. Rev., 2003, 103, 2365-2383.
    • (2003) Chem. Rev. , vol.103 , pp. 2365-2383
    • Wei, C.-C.1    Crane, B.R.2    Stuehr, D.J.3
  • 73
    • 0032488596 scopus 로고    scopus 로고
    • Comparative functioning of dihydro- And tetrahydropterins in supporting electron transfer, catalysis, and subunit dimerization in inducible nitric oxide synthase
    • A. Presta, U. Siddhanta, C. Wu, N. Sennequier, L. Huang, H. M. Abu-Soud, S. Erzurum and D. J. Stuehr, Comparative functioning of dihydro- and tetrahydropterins in supporting electron transfer, catalysis, and subunit dimerization in inducible nitric oxide synthase, Biochemistry, 1998, 37, 298-310.
    • (1998) Biochemistry , vol.37 , pp. 298-310
    • Presta, A.1    Siddhanta, U.2    Wu, C.3    Sennequier, N.4    Huang, L.5    Abu-Soud, H.M.6    Erzurum, S.7    Stuehr, D.J.8
  • 74
    • 0030948345 scopus 로고    scopus 로고
    • Characterization of bovine endothelial nitric oxide synthase as a homodimer with down-regulated uncoupled NADPH oxidase activity: Tetrahydrobiopterin binding kinetics and role of haem in dimerization
    • B. M. List, B. Klosch, C. Volker, A. C. Gorren, W. C. Sessa, E. R. Werner, W. R. Kukovetz, K. Schmidt and B. Mayer, Characterization of bovine endothelial nitric oxide synthase as a homodimer with down-regulated uncoupled NADPH oxidase activity: tetrahydrobiopterin binding kinetics and role of haem in dimerization, Biochem. J., 1997, 323, 159-165.
    • (1997) Biochem. J. , vol.323 , pp. 159-165
    • List, B.M.1    Klosch, B.2    Volker, C.3    Gorren, A.C.4    Sessa, W.C.5    Werner, E.R.6    Kukovetz, W.R.7    Schmidt, K.8    Mayer, B.9
  • 75
    • 0028302095 scopus 로고
    • The pteridine binding site of brain nitric oxide synthase. Tetrahydrobiopterin binding kinetics, specificity, and allosteric interaction with the substrate domain
    • P. Klatt, M. Schmid, E. Leopold, K. Schmidt, E. R. Werner and B. Mayer, The pteridine binding site of brain nitric oxide synthase. Tetrahydrobiopterin binding kinetics, specificity, and allosteric interaction with the substrate domain, J. Biol. Chem., 1994, 269, 13861-13866.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13861-13866
    • Klatt, P.1    Schmid, M.2    Leopold, E.3    Schmidt, K.4    Werner, E.R.5    Mayer, B.6
  • 76
    • 4344566972 scopus 로고    scopus 로고
    • Update on mechanism and catalytic regulation in the NO synthases
    • D. J. Stuehr, J. Santolini, Z.-Q. Wang, C.-C. Wei and S. Adak, Update on mechanism and catalytic regulation in the NO synthases, J. Biol. Chem., 2004, 279, 36167-36170.
    • (2004) J. Biol. Chem. , vol.279 , pp. 36167-36170
    • Stuehr, D.J.1    Santolini, J.2    Wang, Z.-Q.3    Wei, C.-C.4    Adak, S.5
  • 77
    • 0035805555 scopus 로고    scopus 로고
    • Oxygen reduction by nitric-oxide synthases
    • D. Stuehr, S. Pou and G. M. Rosen, Oxygen reduction by nitric-oxide synthases, J. Biol. Chem., 2001, 276, 14533-14536.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14533-14536
    • Stuehr, D.1    Pou, S.2    Rosen, G.M.3
  • 78
    • 0034714233 scopus 로고    scopus 로고
    • 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
    • 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, J. Biol Chem., 2000, 275, 26150-26157.
    • (2000) J. Biol Chem. , vol.275 , pp. 26150-26157
    • Sagami, I.1    Sato, Y.2    Daff, S.3    Shimizu, T.4
  • 79
    • 0037370208 scopus 로고    scopus 로고
    • 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
    • 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, Arch. Biochem. Biophys., 2003, 411, 83-92.
    • (2003) Arch. Biochem. Biophys. , vol.411 , pp. 83-92
    • Chen, P.F.1    Berka, V.2    Wu, K.K.3
  • 80
    • 0035980234 scopus 로고    scopus 로고
    • Structures of tetrahydrobiopterin binding-site mutants of inducible nitric oxide synthase oxygenase dimer and implicated roles of Trp457
    • M. Aoyagi, A. S. Arvai, S. Ghosh, D. J. Stuehr, J. A. Tainer and E. D. Getzoff, Structures of tetrahydrobiopterin binding-site mutants of inducible nitric oxide synthase oxygenase dimer and implicated roles of Trp457, Biochemistry, 2001, 40, 12826-12832.
    • (2001) Biochemistry , vol.40 , pp. 12826-12832
    • Aoyagi, M.1    Arvai, A.S.2    Ghosh, S.3    Stuehr, D.J.4    Tainer, J.A.5    Getzoff, E.D.6
  • 81
    • 15444375706 scopus 로고    scopus 로고
    • A tryptophan that modulates tetrahydrobiopterin dependent electron transfer in nitric oxide synthase regulates enzyme catalysis by additional mechanisms
    • Z.-Q. Wang, C.-C. Wei, J. Santolini, P. Koustubh, Q. Wang and D. J. Stuehr, A Tryptophan That Modulates Tetrahydrobiopterin Dependent Electron Transfer in Nitric Oxide Synthase Regulates Enzyme Catalysis by Additional Mechanisms, Biochemistry, 2005, 44, 4676-4690.
    • (2005) Biochemistry , vol.44 , pp. 4676-4690
    • Wang, Z.-Q.1    Wei, C.-C.2    Santolini, J.3    Koustubh, P.4    Wang, Q.5    Stuehr, D.J.6
  • 82
    • 0034656107 scopus 로고    scopus 로고
    • Nitric oxide-induced autoinhibition of neuronal nitric oxide synthase in the presence of the autoxidation-resistant pteridine 5-methyltetrahydrobiopterin
    • A. C. Gorren, A. Schrammel, C. Riethmuller, K. Schmidt, D. Koesling, E. R. Werner and B. Mayer, Nitric oxide-induced autoinhibition of neuronal nitric oxide synthase in the presence of the autoxidation-resistant pteridine 5-methyltetrahydrobiopterin, Biochem. J., 2000, 347, 475-484.
    • (2000) Biochem. J. , vol.347 , pp. 475-484
    • Gorren, A.C.1    Schrammel, A.2    Riethmuller, C.3    Schmidt, K.4    Koesling, D.5    Werner, E.R.6    Mayer, B.7
  • 83
    • 0242416195 scopus 로고    scopus 로고
    • Ability of tetrahydrobiopterin analogues to support catalysis by inducible nitric oxide synthase: Formation of a pterin radical is required for enzyme activity
    • A. R. Hurshman, C. Krebs, D. E. Edmondson and M. A. Marletta, Ability of tetrahydrobiopterin analogues to support catalysis by inducible nitric oxide synthase: formation of a pterin radical is required for enzyme activity, Biochemistry, 2003, 42, 13287-13303.
    • (2003) Biochemistry , vol.42 , pp. 13287-13303
    • Hurshman, A.R.1    Krebs, C.2    Edmondson, D.E.3    Marletta, M.A.4
  • 84
    • 0032974932 scopus 로고    scopus 로고
    • Nitric oxide-generated P420 nitric oxide synthase: Characterization and roles for tetrahydrobiopterin and substrate in protecting against or reversing the P420 conversion
    • L. Huang, H. M. Abu-Soud, R. Hille and D. J. Stuehr, Nitric oxide-generated P420 nitric oxide synthase: characterization and roles for tetrahydrobiopterin and substrate in protecting against or reversing the P420 conversion, Biochemistry, 1999, 38, 1912-1920.
    • (1999) Biochemistry , vol.38 , pp. 1912-1920
    • Huang, L.1    Abu-Soud, H.M.2    Hille, R.3    Stuehr, D.J.4
  • 85
    • 0037388770 scopus 로고    scopus 로고
    • Crystal structure of the ascorbate peroxidase-ascorbate complex
    • K. H. Sharp, M. Mewies, P. C. Moody and E. L. Raven, Crystal structure of the ascorbate peroxidase-ascorbate complex, Nat. Struct. Biol., 2003, 10, 303-307.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 303-307
    • Sharp, K.H.1    Mewies, M.2    Moody, P.C.3    Raven, E.L.4
  • 86
    • 9644264047 scopus 로고    scopus 로고
    • Regioselective nitration of tryptophan by a complex between bacterial nitric-oxide synthase and tryptophanyl-tRNA synthetase
    • M. R. Buddha, T. Tao, R. J. Parry and B. R. Crane, Regioselective nitration of tryptophan by a complex between bacterial nitric-oxide synthase and tryptophanyl-tRNA synthetase, J. Biol. Chem., 2004, 279, 49567-49570.
    • (2004) J. Biol. Chem. , vol.279 , pp. 49567-49570
    • Buddha, M.R.1    Tao, T.2    Parry, R.J.3    Crane, B.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.