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Volumn 4, Issue 10, 1997, Pages 827-832

Crystal structure of nitric oxide reductase from denitrifying fungus Fusarium oxysporum

Author keywords

[No Author keywords available]

Indexed keywords

NITRIC OXIDE REDUCTASE;

EID: 0030842613     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb1097-827     Document Type: Article
Times cited : (183)

References (42)
  • 1
    • 0027080129 scopus 로고
    • NO news is good news
    • Culotta, E., & Koshland, D. E. Jr. NO news is good news. Science 258, 1862-1865 (1992).
    • (1992) Science , vol.258 , pp. 1862-1865
    • Culotta, E.1    Koshland Jr., D.E.2
  • 2
    • 0027104253 scopus 로고
    • Biochemistry of nitric oxide and its redoxactivated forms
    • Stamler, J. S., Singel, D. S., Loscalzo, J. Biochemistry of nitric oxide and its redoxactivated forms. Science 258, 1898-1902 (1992).
    • (1992) Science , vol.258 , pp. 1898-1902
    • Stamler, J.S.1    Singel, D.S.2    Loscalzo, J.3
  • 3
    • 0024438672 scopus 로고
    • Immunological identification and distribution of dissimilatory heme cdl and nonheme copper nitrite reductases in denitrifying bacteria
    • Coyne, M. S., Arunakumari, A. A., Averill, R. A., Tiedje, J. M. Immunological identification and distribution of dissimilatory heme cdl and nonheme copper nitrite reductases in denitrifying bacteria. Appl. Environ. Microbiol. 55, 2924-2931 (1989).
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 2924-2931
    • Coyne, M.S.1    Arunakumari, A.A.2    Averill, R.A.3    Tiedje, J.M.4
  • 4
    • 0040949999 scopus 로고
    • Denitrification: A question of the control and organization of electron and ion transport
    • Ferguson, S. J. Denitrification: a question of the control and organization of electron and ion transport. Trends Biochem. Sei. 12, 354-357 (1987).
    • (1987) Trends Biochem. Sei. , vol.12 , pp. 354-357
    • Ferguson, S.J.1
  • 5
    • 0020064009 scopus 로고
    • Denitrification
    • Knowles, R. Denitrification. Microbiol. Rev. 46, 43-70 (1982).
    • (1982) Microbiol. Rev. , vol.46 , pp. 43-70
    • Knowles, R.1
  • 6
    • 0025309975 scopus 로고
    • The nitric oxide reductase of Paracoccus denitrificans
    • Carr, G. J., & Ferguson, S. J. The nitric oxide reductase of Paracoccus denitrificans. Biochem. J. 269, 423-429 (1990).
    • (1990) Biochem. J. , vol.269 , pp. 423-429
    • Carr, G.J.1    Ferguson, S.J.2
  • 7
    • 0026763915 scopus 로고
    • Oxidation of dithiothreitol during turnover of nitric oxide reductase: Evidence for generation of nitroxyl with the enzyme from Paracoccus denitrificans
    • Turk, T., & Hollocher, T. C. Oxidation of dithiothreitol during turnover of nitric oxide reductase: evidence for generation of nitroxyl with the enzyme from Paracoccus denitrificans. Biochem. Biophys. Res. Commun. 183, 983-988 (1992).
    • (1992) Biochem. Biophys. Res. Commun. , vol.183 , pp. 983-988
    • Turk, T.1    Hollocher, T.C.2
  • 8
    • 0028306590 scopus 로고
    • Nitric oxide reductase from Pseudomonas stutzeri, a novel cytochrome be complex, Phospholipid requirement electron paramagnetic resonance and redox properties, fur
    • Kastrau, D. H. W., Heiss, B., Kroneck, P. M. H., Zumft, W. G. Nitric oxide reductase from Pseudomonas stutzeri, a novel cytochrome be complex, Phospholipid requirement electron paramagnetic resonance and redox properties, fur. J. Biochem. 222, 293-303 (1994).
    • (1994) J. Biochem. , vol.222 , pp. 293-303
    • Kastrau, D.H.W.1    Heiss, B.2    Kroneck, P.M.H.3    Zumft, W.G.4
  • 9
    • 0024589146 scopus 로고
    • Soluble, nitrate/nitrite-inducible cytochrome P450 of the fungus Fusarium oxysporum
    • Shoun, H., Suyama, W., Yasui, T. Soluble, nitrate/nitrite-inducible cytochrome P450 of the fungus Fusarium oxysporum. FEBS Lett. 244, 11-14 (1989).
    • (1989) FEBS Lett. , vol.244 , pp. 11-14
    • Shoun, H.1    Suyama, W.2    Yasui, T.3
  • 10
    • 0025737114 scopus 로고
    • Denitrification by the fungus Fusarium oxysporum and involvement of cytochrome P450 in the respiratory nitrite reduction
    • Shoun, H., & Tanimoto, T. Denitrification by the fungus Fusarium oxysporum and involvement of cytochrome P450 in the respiratory nitrite reduction. J. Biol. Chem.266, 11078-11082(1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 11078-11082
    • Shoun, H.1    Tanimoto, T.2
  • 11
    • 0027418338 scopus 로고
    • Cytochrome P450 55A1 (P450dNIR) arts as nitric oxide reductase employing NADH as the direct electron donor
    • Nakahara, K.. Tanimoto, T., Hatano, K., Usuda, K., Shoun, H. Cytochrome P450 55A1 (P450dNIR) arts as nitric oxide reductase employing NADH as the direct electron donor. J. Biol. Chem. 268, 8350-8355 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 8350-8355
    • Nakahara, K.1    Tanimoto, T.2    Hatano, K.3    Usuda, K.4    Shoun, H.5
  • 12
    • 0025871374 scopus 로고
    • Nucleotide sequence of the unique nitrate/nitrite-inducible cytochrome P450 cDNA from Fusarium oxysporum
    • Kizawa, H., Tomura, D., Oda, M., Fukamizu, A., Hoshino, T., Gotoh, O., Yasui, T., Shoun, H. Nucleotide sequence of the unique nitrate/nitrite-inducible cytochrome P450 cDNA from Fusarium oxysporum. J. Biol. Chem. 266, 10632-10637(1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 10632-10637
    • Kizawa, H.1    Tomura, D.2    Oda, M.3    Fukamizu, A.4    Hoshino, T.5    Gotoh, O.6    Yasui, T.7    Shoun, H.8
  • 13
    • 0028963395 scopus 로고
    • Spectroscopic and kinetic studies on reaction of cytochrome P450nor with nitric oxide
    • Shiro, Y., Fujii, M., lizuka, T., Adachi, S., Tsukamoto. K., Nakahara, K., Shoun, H. Spectroscopic and kinetic studies on reaction of cytochrome P450nor with nitric oxide./ Biol. Chem. 270, 1617-1623 (1995).
    • (1995) / Biol. Chem. , vol.270 , pp. 1617-1623
    • Shiro, Y.1    Fujii, M.2    Lizuka, T.3    Adachi, S.4    Tsukamoto, K.5    Nakahara, K.6    Shoun, H.7
  • 14
    • 0023645035 scopus 로고
    • High-resolution crystal structure of cytochrome P450cam
    • Poulos, T. L, Finzel, B. C., Howard, A. J. High-resolution crystal structure of cytochrome P450cam. J. Mol. Biol. 195. 687-700 (1987).
    • (1987) J. Mol. Biol. , vol.195 , pp. 687-700
    • Poulos, T.L.1    Finzel, B.C.2    Howard, A.J.3
  • 15
    • 0024974060 scopus 로고
    • Crystal structure of the carbon monoxide-substratecytochrome P450cam ternary complex
    • Raag, R. & Poulos, T. L. Crystal structure of the carbon monoxide-substratecytochrome P450cam ternary complex. Biochemistry 28, 7586-7592 (1989).
    • (1989) Biochemistry , vol.28 , pp. 7586-7592
    • Raag, R.1    Poulos, T.L.2
  • 16
    • 0027326717 scopus 로고
    • Crystal structure of hemoprotein domain of P450BM3, a prototype for microsomal P450's
    • Ravichandran, K. G., Boddupalli, S. S., Hasemann, C. A., Peterson, J. A., Deisenhofer, J. Crystal structure of hemoprotein domain of P450BM3, a prototype for microsomal P450's. Science 261, 731-736 (1993).
    • (1993) Science , vol.261 , pp. 731-736
    • Ravichandran, K.G.1    Boddupalli, S.S.2    Hasemann, C.A.3    Peterson, J.A.4    Deisenhofer, J.5
  • 17
    • 0028267490 scopus 로고
    • Crystal structure and refinement of cytochrome P450terp at 2.3 a resolution
    • Hasemann, C. A., Ravichandran, K. G., Peterson, J. A., Deisenhofer, J. Crystal structure and refinement of cytochrome P450terp at 2.3 A resolution. J. Mol. Biol. 236, 1169-1185(1994).
    • (1994) J. Mol. Biol. , vol.236 , pp. 1169-1185
    • Hasemann, C.A.1    Ravichandran, K.G.2    Peterson, J.A.3    Deisenhofer, J.4
  • 18
    • 0029586252 scopus 로고
    • Structure of cytochrome P450eryF involved in erythromyciri biosynthesis
    • Cupp-Vickery, J. R. & Poulos, T. L. Structure of cytochrome P450eryF involved in erythromyciri biosynthesis. Nature Struct. Biol. 2, 144-153 (1995).
    • (1995) Nature Struct. Biol. , vol.2 , pp. 144-153
    • Cupp-Vickery, J.R.1    Poulos, T.L.2
  • 20
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative computing project No. 4 The CCP4 suite: programs for protein crystallography. Acta crystallogr. D50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 21
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structure
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., Thronton, J. M. PROCHECK: a program to check the stereochemical quality of protein structure. J. Appl. Crystallogr. 26, 283-291 (1993).
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thronton, J.M.4
  • 23
    • 0002782723 scopus 로고
    • ed, Ortiz de Montellano, P. R. Plenum Press, New York
    • nd Ed) (ed, Ortiz de Montellano, P. R.) 151-180 (Plenum Press, New York; 1995).
    • (1995) nd Ed) , pp. 151-180
    • Peterson, J.A.1    Graham-Lorence, S.E.2
  • 24
    • 0029643786 scopus 로고
    • Structure and function of cytochrome P450: A comparative analysis of three crystal structures
    • Hasemann, C. A., Ravichandran, K. G., Boddupalli, S. S., Peterson, J. A., Deisenhofer, J. Structure and function of cytochrome P450: a comparative analysis of three crystal structures. Structure 3, 41-62 (1995).
    • (1995) Structure , vol.3 , pp. 41-62
    • Hasemann, C.A.1    Ravichandran, K.G.2    Boddupalli, S.S.3    Peterson, J.A.4    Deisenhofer, J.5
  • 25
    • 0028017299 scopus 로고
    • Kinetics and thermodynamics of CO binding to cytochrome P450nor
    • Shiro, Y., Kato, M., lizuka, T., Nakahara, K.. Shoun, H. Kinetics and thermodynamics of CO binding to cytochrome P450nor. Biochemistry 33, 8673-8677(1994).
    • (1994) Biochemistry , vol.33 , pp. 8673-8677
    • Shiro, Y.1    Kato, M.2    Lizuka, T.3    Nakahara, K.4    Shoun, H.5
  • 26
    • 0029082717 scopus 로고
    • Iron-ligand structure and iron redox property of nitric oxide reductase cytochrome P450nor from Fusarium oxysporum: Relevance to Its NO reduction activity
    • Shiro, Y., Fujii, M., Isogai, Y, Adachi, S., lizuka, T., Obayashi, E, Makino, R., Nakahara, R., Shoun, H. Iron-ligand structure and iron redox property of nitric oxide reductase cytochrome P450nor from Fusarium oxysporum: relevance to Its NO reduction activity. Biochemistry 34, 9052-9058 (1995).
    • (1995) Biochemistry , vol.34 , pp. 9052-9058
    • Shiro, Y.1    Fujii, M.2    Isogai, Y.3    Adachi, S.4    Lizuka, T.5    Obayashi, E.6    Makino, R.7    Nakahara, R.8    Shoun, H.9
  • 27
    • 0028959345 scopus 로고
    • Denitrification by the fungus Cylindrocarpon tonkinense: Anaerobic cell growth and two isozyme forms of cytochrome P450nor
    • Usuda, K., Toritsuka, N., Matsuo, Y, Kim, D.-H., Shoun, H. Denitrification by the fungus Cylindrocarpon tonkinense: anaerobic cell growth and two isozyme forms of cytochrome P450nor. Appl. Environ. Microbiol. 61, 883-889 (1995).
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 883-889
    • Usuda, K.1    Toritsuka, N.2    Matsuo, Y.3    Kim, D.-H.4    Shoun, H.5
  • 28
    • 0031035984 scopus 로고    scopus 로고
    • Functional and structural comparison of nitric oxide reductases from denitrifying Cylindrocarpon tonkinense and Fusarium oxysporum
    • Toritsuka, N.. Shoun. H., Singh, U. P., Park, S.-Y, lizuka, T., Shiro, Y. Functional and structural comparison of nitric oxide reductases from denitrifying Cylindrocarpon tonkinense and Fusarium oxysporum. Biochim. Biophys. Actä 1338, 93-99 (1997).
    • (1997) Biochim. Biophys. Actä , vol.1338 , pp. 93-99
    • Shoun H, T.N.1    Singh, U.P.2    Park, S.-Y.3    Lizuka, T.4    Shiro, Y.5
  • 29
    • 0001541099 scopus 로고
    • Uncoupling of the cytochrome P-450cam monooxygenase reaction by a single mutation, threonine-252 to alanine or valine: A possible role of the hydroxy amino acid in oxygen activation
    • Imai, M., Shimada, H., Watanabe. Y, Matsushima-Hibiya, Y., Makino, R., Koga, H., Horiuchi, T., Ishimura, Y. Uncoupling of the cytochrome P-450cam monooxygenase reaction by a single mutation, threonine-252 to alanine or valine: A possible role of the hydroxy amino acid in oxygen activation. Proc. Watl. Acad. Sei. USA 86. 7823-7827 (1989).
    • (1989) Proc. Watl. Acad. Sei. USA , vol.86 , pp. 7823-7827
    • Imai, M.1    Shimada, H.2    Watanabe, Y.3    Matsushima-Hibiya, Y.4    Makino, R.5    Koga, H.6    Horiuchi, T.7    Ishimura, Y.8
  • 30
    • 0026352457 scopus 로고
    • Crystal structure of the cytochrome P- 450cam active site mutant Thr252Ala
    • Raag, R., Martinis, S. A., Sugar, S. G., Poulos, T. L. Crystal structure of the cytochrome P- 450cam active site mutant Thr252Ala. Biochemistry 30 11420-11429(1991).
    • (1991) Biochemistry , vol.30 , pp. 11420-11429
    • Raag, R.1    Martinis, S.A.2    Sugar, S.G.3    Poulos, T.L.4
  • 31
    • 0000589432 scopus 로고
    • Catalytic mechanism of cytochrome P450: Evidence for a distal charge relay
    • Gerber, N. C, & Sugar, S. G. Catalytic mechanism of cytochrome P450: evidence for a distal charge relay. J. Am. Chem. Soc. 114, 8742-8743 (1992).
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 8742-8743
    • Gerber, N.C.1    Sugar, S.G.2
  • 32
    • 0027994378 scopus 로고
    • A role for Asp-251 in cytochrome P450cam oxygen activation
    • Gerber, N. C. & Sugar, S. G. A role for Asp-251 in cytochrome P450cam oxygen activation. J. Biol. Chem. 269, 4260-4266 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 4260-4266
    • Gerber, N.C.1    Sugar, S.G.2
  • 33
    • 0028861062 scopus 로고
    • The role of Thr268 in oxygen activation of cytochrome P450BM3
    • Yeom, H., Sugar, S. G., Li, H., Poulos, T. L, Fulco, A. J. The role of Thr268 in oxygen activation of cytochrome P450BM3. Biochemistry 34, 14733-14740 (1995).
    • (1995) Biochemistry , vol.34 , pp. 14733-14740
    • Yeom, H.1    Sugar, S.G.2    Li, H.3    Poulos, T.L.4    Fulco, A.J.5
  • 34
    • 0030004641 scopus 로고    scopus 로고
    • Investigation of the proton-assisted pathway to formation of the catalytically active, ferryl species of P450s by molecular dynamics studies of P450eryF
    • Harris, D. L, & Loew, G. H. J. Investigation of the proton-assisted pathway to formation of the catalytically active, ferryl species of P450s by molecular dynamics studies of P450eryF. J. Am. Chem. Soc. 118. 6377-6387 (1996).
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 6377-6387
    • Harris, D.L.1    Loew, G.H.J.2
  • 35
    • 0030879011 scopus 로고    scopus 로고
    • Crystallization, Preliminary Diffraction and Electron Paramagnetic Resonance Studies of a Single Crystal of Cytochrome P450nor
    • Park. S.-Y. Shimizu, H., Adachi, S.-i., Shiro, Y, lizuka. T., Nakagawa, A., Tanaka, I., Shoun, H., Hori, H. Crystallization, Preliminary Diffraction and Electron Paramagnetic Resonance Studies of a Single Crystal of Cytochrome P450nor. FEBS Lett. 412, 346-350(1997).
    • (1997) FEBS Lett. , vol.412 , pp. 346-350
    • Park, S.-Y.1    Shimizu, H.2    Adachi, S.-I.3    Shiro, Y.4    Lizuka, T.5    Nakagawa, A.6    Tanaka, I.7    Shoun, H.8    Hori, H.9
  • 36
    • 0000525517 scopus 로고
    • A focusing weissenberg camera with multi-layer-line screens for macromolecular crystallography
    • Sakabe, N. A focusing weissenberg camera with multi-layer-line screens for macromolecular crystallography. J./ppl.Crysral/ogr. 16, 542-547(1983).
    • (1983) J./ppl.Crysral/ogr. , vol.16 , pp. 542-547
    • Sakabe, N.1
  • 37
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • L. Sawyer, N. Isaace & S. Bailey, eds
    • Otwinowski, Z. Oscillation data reduction program. In Data collection and processing (L. Sawyer, N. Isaace & S. Bailey, eds) 56-62 (SERC Daresbury Laboratory, Warrington, UK; 1993).
    • (1993) Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 38
    • 0028114231 scopus 로고
    • Structure at 2.8 a resolution of F1-ATPase fom bovine heart mitochondria
    • Abrahams, J. P., Leliew, A. G. W., Lutter, R., Walker, J. E. Structure at 2.8 A resolution of F1-ATPase fom bovine heart mitochondria. Nature 370, 621-623 (1994).
    • (1994) Nature , vol.370 , pp. 621-623
    • Abrahams, J.P.1    Leliew, A.G.W.2    Lutter, R.3    Walker, J.E.4
  • 39
    • 84889120137 scopus 로고
    • Improved method for building protein models in electron density maps and location of errors in these models
    • Jones, T. A., Zou, J. Y, Cowan, S. W., Kjeldgaard, M. Improved method for building protein models in electron density maps and location of errors in these models. Acta Crystallogr. A47, 110-119 (1991).
    • (1991) Acta Crystallogr. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 41
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to protuce both de tailed and schematic plots of protein structures
    • Kraulis, P. J. MOLSCRIPT: a program to protuce both de tailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 42
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three-dimentional solid model representations of macromolecules
    • Evans, S. V. SETOR: hardware lighted three-dimentional solid model representations of macromolecules. J. Mol. Graphics 11, 134-1338 (1993).
    • (1993) J. Mol. Graphics , vol.11 , pp. 134-1338
    • Evans, S.V.1


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