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Volumn 5, Issue 7, 1998, Pages 355-364

The high-potential flavin and heme of nitric oxide synthase are not magnetically linked: Implications for electron transfer

Author keywords

Electron paramagnetic resonance; Electron transfer; Flavin; Heme

Indexed keywords

ANIMALIA;

EID: 0032125851     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(98)90069-2     Document Type: Article
Times cited : (19)

References (27)
  • 1
    • 0029858301 scopus 로고    scopus 로고
    • PIN: Protein inhibitor of neuronal NOS
    • Jaffrey, S.R. & Snyder, S.H. (1996). PIN: protein inhibitor of neuronal NOS. Science 274, 774-776.
    • (1996) Science , vol.274 , pp. 774-776
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 2
    • 0028026868 scopus 로고
    • Nitric oxide synthase: Aspects concerning structure and catalysis
    • Marletta, M.A. (1994). Nitric oxide synthase: aspects concerning structure and catalysis. Cell 78, 927-930.
    • (1994) Cell , vol.78 , pp. 927-930
    • Marletta, M.A.1
  • 4
    • 0028882828 scopus 로고
    • Interaction of calmodulin with the inducible murine macrophage nitric oxide synthase
    • Stevens-Truss, R. & Marletta, M.A. (1995). Interaction of calmodulin with the inducible murine macrophage nitric oxide synthase. Biochemistry 34, 15638-15645.
    • (1995) Biochemistry , vol.34 , pp. 15638-15645
    • Stevens-Truss, R.1    Marletta, M.A.2
  • 5
    • 0027325255 scopus 로고
    • Nitric oxide synthase structure and mechanism
    • Marietta, M.A. (1993). Nitric oxide synthase structure and mechanism. J. Biol. Chem. 268, 12231-12234.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12231-12234
    • Marietta, M.A.1
  • 6
    • 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. & Masters, B.S.S. (1992) Cloned, expressed rat cerebellar nitric oxide synthase contains stoichiometric amounts of heme, which binds carbon monoxide. Proc. Natl Acad. Sci. USA 89, 11141-11145.
    • (1992) Proc. Natl Acad. Sci. USA , 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.S.6
  • 7
    • 0026660191 scopus 로고
    • Spectral characterization of brain and macrophage nitric oxide syntheses
    • Stuehr, D.J. & Ikeda-Saito, M. (1992). Spectral characterization of brain and macrophage nitric oxide syntheses. J. Biol. Chem. 267, 20547-20550.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20547-20550
    • Stuehr, D.J.1    Ikeda-Saito, M.2
  • 8
    • 0026735580 scopus 로고
    • Nitric oxide synthase is a cytochrome P-450 type hemoprotein
    • White, K.A. & Marietta, 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    Marietta, M.A.2
  • 9
    • 11544309187 scopus 로고
    • Purification of the inducible murine macrophage nitric oxide synthase: Identification as a flavoprotein and detection of enzyme-bound tetrahydrobiopterin
    • (Moncada, S., Marietta, M.A., Hibbs Jr, J.B. & Higgs, E.A., eds), Portland Press. London
    • Hevel, J.M., White, K.A. & Marietta, M.A. (1992). Purification of the inducible murine macrophage nitric oxide synthase: identification as a flavoprotein and detection of enzyme-bound tetrahydrobiopterin. In The Biology of Nitric Oxide. (Moncada, S., Marietta, M.A., Hibbs Jr, J.B. & Higgs, E.A., eds), pp. 19-21, Portland Press. London.
    • (1992) The Biology of Nitric Oxide , pp. 19-21
    • Hevel, J.M.1    White, K.A.2    Marietta, M.A.3
  • 10
    • 0025787205 scopus 로고
    • Purification and characterization of the cytokine-induced macrophage nitric oxide synthase: An FAD- and FMN-containing flavoprotein
    • Stuehr, D.J., Cho, HJ., Kwon, N.S., Weise, M.F. & Nathan, C.F. (1991). Purification and characterization of the cytokine-induced macrophage nitric oxide synthase: an FAD- and FMN-containing flavoprotein. Proc. Natl Acad. Sci. USA 88, 7773-7777.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 7773-7777
    • Stuehr, D.J.1    Cho, H.J.2    Kwon, N.S.3    Weise, M.F.4    Nathan, C.F.5
  • 11
    • 0026746287 scopus 로고
    • Macrophage nitric oxide synthase: Relationship between enzyme-bound tetrahydrobiopterin and synthase activity
    • Hevel, J.M. & Marietta, M.A. (1992). Macrophage nitric oxide synthase: relationship between enzyme-bound tetrahydrobiopterin and synthase activity. Biochemistry 31, 7160-7165.
    • (1992) Biochemistry , vol.31 , pp. 7160-7165
    • Hevel, J.M.1    Marietta, M.A.2
  • 12
    • 0028601409 scopus 로고
    • Characterization of neuronal nitric oxide synthase and a C415H mutant, purified from a baculovirus overexpression system
    • Richards, M.K. & Marletta, M.A. (1994) Characterization of neuronal nitric oxide synthase and a C415H mutant, purified from a baculovirus overexpression system. Biochemistry 33, 14723-14732.
    • (1994) Biochemistry , vol.33 , pp. 14723-14732
    • Richards, M.K.1    Marletta, M.A.2
  • 13
    • 0028276990 scopus 로고
    • Evidence for a biodomain structure of constitutive cerebellar nitric oxide synthase
    • Sheta, E.A., McMillan, K. & Masters, B.S.S. (1994). Evidence for a biodomain structure of constitutive cerebellar nitric oxide synthase. J. Biol. Chem. 269, 15147-15153.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15147-15153
    • Sheta, E.A.1    McMillan, K.2    Masters, B.S.S.3
  • 14
    • 0018220868 scopus 로고
    • Identification of the high and low potential flavins of liver microsomal NADPH-cytochrome P-450 reductase
    • Vermilion, J.L & Coon, M.J. (1978). Identification of the high and low potential flavins of liver microsomal NADPH-cytochrome P-450 reductase. J. Biol. Chem. 253, 8812-8819.
    • (1978) J. Biol. Chem. , vol.253 , pp. 8812-8819
    • Vermilion, J.L.1    Coon, M.J.2
  • 16
  • 17
    • 0027379671 scopus 로고
    • Intrinsic and extrinsic paramagnets as probes of metal clusters
    • Hales, B.J. (1993). Intrinsic and extrinsic paramagnets as probes of metal clusters. Methods Enzymol. 227, 384-395.
    • (1993) Methods Enzymol. , vol.227 , pp. 384-395
    • Hales, B.J.1
  • 18
    • 12644253700 scopus 로고    scopus 로고
    • Characterization of endothelial nitric-oxide synthase and its reaction with ligand by electron paramagnetic resonance spectroscopy
    • Tsai, A.-L., Berka, V., Chen, P.-F. & Palmer, G. (1996). Characterization of endothelial nitric-oxide synthase and its reaction with ligand by electron paramagnetic resonance spectroscopy. J. Biol. Chem. 271, 32563-32571.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32563-32571
    • Tsai, A.-L.1    Berka, V.2    Chen, P.-F.3    Palmer, G.4
  • 19
    • 0028913561 scopus 로고
    • Spectroscopic evidence for the symmetric location of tyrosines D and Z in photosystem II
    • Koulougliotis, D., Tang, X.-S., Diner, B.A. & Brudvig, G.W. (1995). Spectroscopic evidence for the symmetric location of tyrosines D and Z in photosystem II. Biochemistry 34, 2850-2856.
    • (1995) Biochemistry , vol.34 , pp. 2850-2856
    • Koulougliotis, D.1    Tang, X.-S.2    Diner, B.A.3    Brudvig, G.W.4
  • 20
    • 0028582164 scopus 로고
    • Calmodulin controls neuronal nitric-oxide synthase by a dual mechanism
    • Abu-Soud, H.M., Yoho, L.L. & Stuehr, D.J. (1994). Calmodulin controls neuronal nitric-oxide synthase by a dual mechanism. J. Biol. Chem. 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
  • 21
    • 0019876977 scopus 로고
    • Thermodynamic and electron paramagnetic resonance characterization of flavin in succinate dehydrogenase
    • Ohnishi, T., King, I.E., Salerno, J.C., Blum, H., Bowyer, J.R. & Maida, T. (1981). Thermodynamic and electron paramagnetic resonance characterization of flavin in succinate dehydrogenase. J. Biol. Chem. 256, 5577-5582.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5577-5582
    • Ohnishi, T.1    King, I.E.2    Salerno, J.C.3    Blum, H.4    Bowyer, J.R.5    Maida, T.6
  • 22
    • 0027500817 scopus 로고
    • Electron paramagnetic resonance spectroscopy of iron complexes and iron-containing proteins
    • Cammack, R. & Cooper, C.E. (1993). Electron paramagnetic resonance spectroscopy of iron complexes and iron-containing proteins. Methods Enzymol. 227, 353-384.
    • (1993) Methods Enzymol. , vol.227 , pp. 353-384
    • Cammack, R.1    Cooper, C.E.2
  • 23
    • 0030723329 scopus 로고    scopus 로고
    • The structure of nitric oxide synthase oxygenase domain and inhibitor complexes
    • Crane, B.R., et al., & Tainer, J.A. (1997). The structure of nitric oxide synthase oxygenase domain and inhibitor complexes. Science 278, 425-431.
    • (1997) Science , vol.278 , pp. 425-431
    • Crane, B.R.1    Tainer, J.A.2
  • 26
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S.N., Hunt, H.D., Horton, R.M., Pullen, J.K. & Pease, LR. (1989). Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.