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Volumn 48, Issue 43, 2009, Pages 10246-10254

Single crystal structural and absorption spectral characterizations of nitric oxide synthase complexed with Nω-hydroxy-L-arginine and diatomic ligands

Author keywords

[No Author keywords available]

Indexed keywords

CITRULLINE; DIOXYGENS; GUANIDINIUM; L-ARGININE; LIGAND COMPLEXES; NEURONAL NITRIC-OXIDE SYNTHASE (NNOS); NITRIC-OXIDE SYNTHASE; OH GROUP; PROTONATED; REDOX STATE; SOLVENT STRUCTURES; SPECTRAL CHARACTERIZATION; X-RAY DIFFRACTION DATA COLLECTION; X-RAY STRUCTURE;

EID: 70350508407     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9009743     Document Type: Article
Times cited : (19)

References (41)
  • 1
    • 0025883342 scopus 로고
    • Nitric oxide: Physiology, pathophysiology, and pharmacology
    • Moncada, S., Palmer, R. M., and Higgs, E. A. (1991) Nitric oxide: physiology, pathophysiology, and pharmacology. Pharmacol. Rev. 43, 109-142.
    • (1991) Pharmacol. Rev. , vol.43 , pp. 109-142
    • Moncada, S.1    Palmer, R.M.2    Higgs, E.A.3
  • 4
    • 0000872980 scopus 로고    scopus 로고
    • Structural themes determining function in nitric oxide synthases
    • (Kadish, K. M., Smith, K. M., and Guilard, R., Eds.) Acadamic Press, San Diego, CA
    • Raman, C. S., Martasek, P., and Masters, B. S. S. (2000) Structural themes determining function in nitric oxide synthases, in The porphyrin handbook (Kadish, K. M., Smith, K. M., and Guilard, R., Eds.) pp 293-339, Acadamic Press, San Diego, CA.
    • (2000) The Porphyrin Handbook , pp. 293-339
    • Raman, C.S.1    Martasek, P.2    Masters, B.S.S.3
  • 6
    • 0027525273 scopus 로고
    • Nitric oxide synthases reveal a role for calmodulin in controlling electron transfer
    • Abu-Soud, H. M., and Stuehr, D. J. (1993) Nitric oxide synthases reveal a role for calmodulin in controlling electron transfer. Proc. Natl. Acad. Sci. U.S.A. 90, 10769-10772.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 10769-10772
    • Abu-Soud, H.M.1    Stuehr, D.J.2
  • 7
    • 0028170425 scopus 로고
    • L-arginine and calmodulin regulation of the heme iron reactivity in neuronal nitric oxide synthase
    • Matsuoka, A., Stuehr, D. J., Olson, J. S., Clark, P., and Ikeda-Saito, M. (1994) L-arginine and calmodulin regulation of the heme iron reactivity in neuronal nitric oxide synthase. J. Biol. Chem. 269, 20335-20339.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20335-20339
    • Matsuoka, A.1    Stuehr, D.J.2    Olson, J.S.3    Clark, P.4    Ikeda-Saito, M.5
  • 8
    • 0032571411 scopus 로고    scopus 로고
    • Structure of nitric oxide synthase oxygenase dimer with pterin and substrate
    • DOI 10.1126/science.279.5359.2121
    • Crane, B. R., Arvai, A. S., Ghosh, D. K., Wu, C., Getzoff, E. D., Stuehr, D. J., and Tainer, J. A. (1998) Structure of nitric oxide synthase oxygenase dimer with pterin and substrate. Science 279, 2121-2126. (Pubitemid 28196359)
    • (1998) Science , vol.279 , Issue.5359 , pp. 2121-2126
    • Crane, B.R.1    Arvai, A.S.2    Ghosh, D.K.3    Wu, C.4    Getzoff, E.D.5    Stuehr, D.J.6    Tainer, J.A.7
  • 9
    • 0032416666 scopus 로고    scopus 로고
    • Crystal structure of constitutive endothelial nitric oxide synthase: A paradigm for pterin function involving a novel metal center
    • DOI 10.1016/S0092-8674(00)81718-3
    • Raman, C. S., Li, H., Martasek, P., Kral, V., Masters, B. S., and Poulos, T. L. (1998) Crystal structure of constitutive endothelial nitric oxide synthase: a paradigm for pterin function involving a novel metal center. Cell 95, 939-950. (Pubitemid 29019046)
    • (1998) Cell , vol.95 , Issue.7 , pp. 939-950
    • Raman, C.S.1    Li, H.2    Martasek, P.3    Kral, V.4    Masters, B.S.S.5    Poulos, T.L.6
  • 10
    • 0026471538 scopus 로고
    • Cloned, expressed rat cerebellar nitric oxide synthase contains stoichiometric amounts of heme, which binds carbon monoxide
    • McMillan, K., Bredt, D. S., Hirsch, D. J., Snyder, S. H., Clark, J. E., and Masters, B. S. (1992) Cloned, expressed rat cerebellar nitric oxide synthase contains stoichiometric amounts of heme, which binds carbon monoxide. Proc. Natl. Acad. Sci. U.S.A. 89, 11141-11145.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 11141-11145
    • McMillan, K.1    Bredt, D.S.2    Hirsch, D.J.3    Snyder, S.H.4    Clark, J.E.5    Masters, B.S.6
  • 11
    • 0026735580 scopus 로고
    • Nitric oxide synthase is a cytochrome P-450 type hemoprotein
    • White, K. A., and Marletta, M. A. (1992) Nitric oxide synthase is a cytochrome P-450 type hemoprotein. Biochemistry 31, 6627-6631.
    • (1992) Biochemistry , vol.31 , pp. 6627-6631
    • White, K.A.1    Marletta, M.A.2
  • 12
    • 0026660191 scopus 로고
    • Spectral characterization of brain and macrophage nitric oxide synthases. Cytochrome P-450-like hemeproteins that contain a flavin semiquinone radical
    • Stuehr, D. J., and Ikeda-Saito, M. (1992) Spectral characterization of brain and macrophage nitric oxide synthases. Cytochrome P-450-like hemeproteins that contain a flavin semiquinone radical. J. Biol. Chem. 267, 20547-20550.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20547-20550
    • Stuehr, D.J.1    Ikeda-Saito, M.2
  • 13
    • 33746257423 scopus 로고    scopus 로고
    • Structural studies of constitutive nitric oxide synthases with diatomic ligands bound
    • Li, H., Igarashi, J., Jamal, J., Yang, W., and Poulos, T. L. (2006) Structural studies of constitutive nitric oxide synthases with diatomic ligands bound. J. Biol. Inorg. Chem. 11, 753-768.
    • (2006) J. Biol. Inorg. Chem. , vol.11 , pp. 753-768
    • Li, H.1    Igarashi, J.2    Jamal, J.3    Yang, W.4    Poulos, T.L.5
  • 14
    • 33846050557 scopus 로고    scopus 로고
    • Cryoradiolytic reduction of crystalline heme proteins: Analysis by UV-Vis spectroscopy and X-ray crystallography
    • DOI 10.1107/S0909049506049806
    • Beitlich, T., Kuhnel, K., Schulze-Briese, C., Shoeman, R. L., and Schlichting, I. (2007) Cryoradiolytic reduction of crystalline heme proteins: analysis by UV-Vis spectroscopy and X-ray crystallography. J. Synchrotron Radiat. 14, 11-23. (Pubitemid 46058902)
    • (2007) Journal of Synchrotron Radiation , vol.14 , Issue.1 , pp. 11-23
    • Seitlich, T.1    Kuhnel, K.2    Schulze-Briese, C.3    Shoeman, R.L.4    Schlichting, I.5
  • 15
    • 18744415136 scopus 로고    scopus 로고
    • The novel binding mode of N-alkyl-N′-hydroxyguanidine to neuronal nitric oxide synthase provides mechanistic insights into NO biosynthesis
    • DOI 10.1021/bi020417c
    • Li, H., Shimizu, H., Flinspach, M., Jamal, J., Yang, W., Xian, M., Cai, T., Wen, E. Z., Jia, Q., Wang, P. G., and Poulos, T. L. (2002) The novel binding mode of N-alkyl-N′-hydroxyguanidine to neuronal nitric oxide synthase provides mechanistic insights into NO biosynthesis. Biochemistry 41, 13868-13875. (Pubitemid 35364860)
    • (2002) Biochemistry , vol.41 , Issue.47 , pp. 13868-13875
    • Li, H.1    Shimizu, H.2    Flinspach, M.3    Jamal, J.4    Yang, W.5    Xian, M.6    Cai, T.7    Wen, E.Z.8    Jia, Q.9    Wang, P.G.10    Poulos, T.L.11
  • 16
    • 0027728765 scopus 로고
    • A fast and portable microspectrophometer for protein crystallography
    • Hadfield, A., and Hajdu, J. (1993) A fast and portable microspectrophometer for protein crystallography. J. Appl. Crystallogr. 26, 839-842.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 839-842
    • Hadfield, A.1    Hajdu, J.2
  • 17
    • 33846085666 scopus 로고    scopus 로고
    • Tracking X-ray-derived redox changes in crystals of a methylamine dehydrogenase/amicyanin complex using single-crystal UV/Vis microspectrophotometry
    • DOI 10.1107/S0909049506051259
    • Pearson, A. R., Pahl, R., Kovaleva, E. G., Davidson, V. L., and Wilmot, C. M. (2007) Tracking X-ray-derived redox changes in crystals of a methylamine dehydrogenase/amicyanin complex using single-crystal UV/Vis microspectrophotometry. J. Synchrotron Radiat. 14, 92-98. (Pubitemid 46058909)
    • (2007) Journal of Synchrotron Radiation , vol.14 , Issue.1 , pp. 92-98
    • Pearson, A.R.1    Pahl, R.2    Kovaleva, E.G.3    Davidson, V.L.4    Wilmot, C.M.5
  • 18
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26, 795-800.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 19
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D50, 760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 20
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D53, 240-255.
    • (1997) Acta Crystallogr. , vol.D53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 21
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn, M. D., Isupov, M. N., and Murshudov, G. N. (2001) Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr. D57, 122-133.
    • (2001) Acta Crystallogr. , vol.D57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 24
    • 84889120137 scopus 로고
    • Improved methods for building models in electron density and the location of errors in these models
    • Jones, T. A., Zou, J.-Y., Cowan, S. W., and Kjeldgaarrd, M. (1991) Improved methods for building models in electron density and the location of errors in these models. Acta crystallogr. A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaarrd, M.4
  • 27
    • 0034716344 scopus 로고    scopus 로고
    • Theoretical studies on NG-hydroxy-L-arginine and derived radicals: Implications for the mechanism of nitric oxide synthase
    • Tantillo, D. J., Fukuto, J. M., Hoffman, B. M., Silverman, R. B., and Houk, K. N. (2000) Theoretical studies on NG-hydroxy-L-arginine and derived radicals: implications for the mechanism of nitric oxide synthase. J. Am. Chem. Soc. 122, 536-537.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 536-537
    • Tantillo, D.J.1    Fukuto, J.M.2    Hoffman, B.M.3    Silverman, R.B.4    Houk, K.N.5
  • 28
    • 15444379675 scopus 로고    scopus 로고
    • S-nitrosation and regulation of inducible nitric oxide synthase
    • DOI 10.1021/bi0474463
    • Mitchell, D. A., Erwin, P. A., Michel, T., and Marletta, M. A. (2005) S-Nitrosation and regulation of inducible nitric oxide synthase. Biochemistry 44, 4636-4647. (Pubitemid 40396742)
    • (2005) Biochemistry , vol.44 , Issue.12 , pp. 4636-4647
    • Mitchell, D.A.1    Erwin, P.A.2    Michel, T.3    Marletta, M.A.4
  • 29
    • 33644515338 scopus 로고    scopus 로고
    • Nitrosyl-heme structures of Bacillus subtilis nitric oxide synthase have implications for understanding substrate oxidation
    • DOI 10.1021/bi0518848
    • Pant, K., and Crane, B. R. (2006) Nitrosyl-heme structures of Bacillus subtilis nitric oxide synthase have implications for understanding substrate oxidation. Biochemistry 45, 2537-2544. (Pubitemid 43298031)
    • (2006) Biochemistry , vol.45 , Issue.8 , pp. 2537-2544
    • Pant, K.1    Crane, B.R.2
  • 30
    • 0027325255 scopus 로고
    • Nitric oxide synthase structure and mechanism
    • Marletta, M. A. (1993) Nitric oxide synthase structure and mechanism. J. Biol. Chem. 268, 12231-12234.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12231-12234
    • Marletta, M.A.1
  • 31
    • 0028234359 scopus 로고
    • On the mechanism of the nitric oxide synthase-catalyzed conversion of N omega-hydroxyl-L-arginine to citrulline and nitric oxide
    • Korth, H. G., Sustmann, R., Thater, C., Butler, A. R., and Ingold, K. U. (1994) On the mechanism of the nitric oxide synthase-catalyzed conversion of N omega-hydroxyl-L-arginine to citrulline and nitric oxide. J. Biol. Chem. 269, 17776-17779.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17776-17779
    • Korth, H.G.1    Sustmann, R.2    Thater, C.3    Butler, A.R.4    Ingold, K.U.5
  • 32
    • 0028902552 scopus 로고
    • Nitric oxide synthases: Properties and catalytic mechanism
    • Griffith, O. W., and Stuehr, D. J. (1995) Nitric oxide synthases: properties and catalytic mechanism. Annu. Rev. Physiol. 57, 707-736.
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 707-736
    • Griffith, O.W.1    Stuehr, D.J.2
  • 33
    • 0033596911 scopus 로고    scopus 로고
    • G-hydroxy-L-arginine bound to holo-neuronal nitric oxide synthase
    • Tierney, D. L., Huang, H., Martasek, P., Masters, B. S., Silverman, R. B., and Hoffman, B. M. (1999) ENDOR spectroscopic evidence for the position and structure of NG-hydroxy-L-arginine bound to holoneuronal nitric oxide synthase. Biochemistry 38, 3704-3710. (Pubitemid 129514626)
    • (1999) Biochemistry , vol.38 , Issue.12 , pp. 3704-3710
    • Tierney, D.L.1    Huang, H.2    Martasek, P.3    Masters, B.S.S.4    Silverman, R.B.5    Hoffman, B.M.6
  • 34
    • 0034712677 scopus 로고    scopus 로고
    • Structures of the N(omega)-hydroxy-L-arginine complex of inducible nitric oxide synthase oxygenase dimer with active and inactive pterins
    • DOI 10.1021/bi992409a
    • Crane, B. R., Arvai, A. S., Ghosh, S., Getzoff, E. D., Stuehr, D. J., and Tainer, J. A. (2000) Structures of the N(omega)-hydroxy-L-arginine complex of inducible nitric oxide synthase oxygenase dimer with active and inactive pterins. Biochemistry 39, 4608-4621. (Pubitemid 30225324)
    • (2000) Biochemistry , vol.39 , Issue.16 , pp. 4608-4621
    • Crane, B.R.1    Arvai, A.S.2    Ghosh, S.3    Getzoff, E.D.4    Stuehr, D.J.5    Tainer, J.A.6
  • 35
    • 0034833563 scopus 로고    scopus 로고
    • Mechanism of nitric oxide synthase. Evidence that direct hydrogen atom abstraction from the O-H bond of NG-hydroxyarginine is not relevant to the mechanism
    • Huang, H., Hah, J. M., and Silverman, R. B. (2001) Mechanism of nitric oxide synthase. Evidence that direct hydrogen atom abstraction from the O-H bond of NG-hydroxyarginine is not relevant to the mechanism. J. Am. Chem. Soc. 123, 2674-2676.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 2674-2676
    • Huang, H.1    Hah, J.M.2    Silverman, R.B.3
  • 38
    • 0345306661 scopus 로고    scopus 로고
    • A tetrahydrobiopterin radical forms and then becomes reduced during N{omega}-hydroxyarginine oxidation by nitric-oxide synthase
    • Wei, C. C., Wang, Z. Q., Hemann, C., Hille, R., and Stuehr, D. J. (2003)A tetrahydrobiopterin radical forms and then becomes reduced during N{omega}-hydroxyarginine oxidation by nitric-oxide synthase. J. Biol. Chem. 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
  • 39
    • 0034721839 scopus 로고    scopus 로고
    • Arginine conversion to nitroxide by tetrahydrobiopterin-free neuronal nitric-oxide synthase. Implications for mechanism
    • Adak, S., Wang, Q., and Stuehr, D. J. (2000) Arginine conversion to nitroxide by tetrahydrobiopterin-free neuronal nitric-oxide synthase. Implications for mechanism. J. Biol. Chem. 275, 33554-33561.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33554-33561
    • Adak, S.1    Wang, Q.2    Stuehr, D.J.3
  • 40
    • 34249776667 scopus 로고    scopus 로고
    • Substrate- And isoform-specific dioxygen complexes of nitric oxide synthase
    • Li, D., Kabir, M., Stuehr, D. J., Rousseau, D. L., and Yeh, S. R. (2007) Substrate- and isoform-specific dioxygen complexes of nitric oxide synthase. J. Am. Chem. Soc. 129, 6943-6951.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 6943-6951
    • Li, D.1    Kabir, M.2    Stuehr, D.J.3    Rousseau, D.L.4    Yeh, S.R.5
  • 41
    • 34547104822 scopus 로고    scopus 로고
    • Substrate-specific interactions with the heme-bound oxygen molecule of nitric-oxide synthase
    • Chartier, F. J., and Couture, M. (2007) Substrate-specific interactions with the heme-bound oxygen molecule of nitric-oxide synthase. J. Biol. Chem. 282, 20877-20886.
    • (2007) J. Biol. Chem. , vol.282 , pp. 20877-20886
    • Chartier, F.J.1    Couture, M.2


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