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Volumn 369, Issue 1, 2003, Pages 77-88

Crystal structure of nitrous oxide reductase from Paracoccus denitrificans at 1.6 Å resolution

Author keywords

Bridging sulphide; Chloride; Copper protein; CuA; CuZ; Denitrification

Indexed keywords

BACTERIA; CALCIUM; COPPER; CRYSTAL STRUCTURE; CYANIDES; ENZYMES; NITROGEN COMPOUNDS; PROTEINS;

EID: 0037270324     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20020782     Document Type: Article
Times cited : (139)

References (57)
  • 1
    • 0031456471 scopus 로고    scopus 로고
    • Cell biology and molecular basis of denitrification
    • Zumft, W. G. (1997) Cell biology and molecular basis of denitrification. Microbiol. Mol. Biol. Rev. 61, 533-616
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 533-616
    • Zumft, W.G.1
  • 3
    • 0034676427 scopus 로고    scopus 로고
    • Global change. It's not a gas
    • Bange, H. W. (2000) Global change. It's not a gas. Nature (London) 408, 301-302
    • (2000) Nature (London) , vol.408 , pp. 301-302
    • Bange, H.W.1
  • 6
    • 0024267905 scopus 로고
    • The cupric site in nitrous oxide reductase contains a mixed valence [Cu(II), Cu(I)] binuclear centre: A multifrequency electron paramagnetic resonance investigation
    • Kroneck, P. M. H., Antholine, W. E., Riester, J. and Zumft, W. G. (1988) The cupric site in nitrous oxide reductase contains a mixed valence [Cu(II), Cu(I)] binuclear centre: a multifrequency electron paramagnetic resonance investigation. FEBS Lett. 242, 70-74
    • (1988) FEBS Lett. , vol.242 , pp. 70-74
    • Kroneck, P.M.H.1    Antholine, W.E.2    Riester, J.3    Zumft, W.G.4
  • 8
    • 0028226882 scopus 로고
    • Cytochrome oxidase evolved by tinkering with denitrification enzymes
    • Saraste, M. and Castresana, J. (1994) Cytochrome oxidase evolved by tinkering with denitrification enzymes. FEBS Lett. 341, 1-4
    • (1994) FEBS Lett. , vol.341 , pp. 1-4
    • Saraste, M.1    Castresana, J.2
  • 9
    • 0035957058 scopus 로고    scopus 로고
    • A novel copper A containing menaquinol NO reductase from Bacillus azotoformans
    • Suharti, Strampraad, M. J. F., Schroder, I. and de Vries, S. (2001). A novel copper A containing menaquinol NO reductase from Bacillus azotoformans Biochemistry 40, 2632-2639
    • (2001) Biochemistry , vol.40 , pp. 2632-2639
    • Suharti1    Strampraad, M.J.F.2    Schroder, I.3    De Vries, S.4
  • 10
    • 0030886203 scopus 로고    scopus 로고
    • Structure at 2.7 Å resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody Fv fragment
    • Ostermeier, C., Harenga, A., Ermler, U. and Michel, H. (1997) Structure at 2.7 Å resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody Fv fragment. Proc. Natl. Acad. Sci. U.S.A. 94, 10547-10553
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 10547-10553
    • Ostermeier, C.1    Harenga, A.2    Ermler, U.3    Michel, H.4
  • 13
    • 0029558330 scopus 로고
    • Crystal structure of the membrane-exposed domain from a respiratory quinol oxidase complex with an engineered dinuclear copper centre
    • Willmanns, M., Lappalainen, P., Kelly, M., Sauer-Eriksson, E. and Saraste, M. (1995) Crystal structure of the membrane-exposed domain from a respiratory quinol oxidase complex with an engineered dinuclear copper centre. Proc. Natl. Acad. Sci. U.S.A. 92, 11955-11959
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 11955-11959
    • Willmanns, M.1    Lappalainen, P.2    Kelly, M.3    Sauer-Eriksson, E.4    Saraste, M.5
  • 20
    • 0025934978 scopus 로고
    • A model of the copper centres of nitrous oxide reductase (Pseudomonas stutzeri). Evidence from optical, EPR and MCD spectroscopy
    • Farrar, J. A., Thomson, A. J., Cheesman, M. R., Dooley, D. M. and Zumft, W. G. (1991) A model of the copper centres of nitrous oxide reductase (Pseudomonas stutzeri). Evidence from optical, EPR and MCD spectroscopy. FEBS Lett. 294, 11-15
    • (1991) FEBS Lett. , vol.294 , pp. 11-15
    • Farrar, J.A.1    Thomson, A.J.2    Cheesman, M.R.3    Dooley, D.M.4    Zumft, W.G.5
  • 21
    • 0039619862 scopus 로고    scopus 로고
    • Purification, characterization, and preliminary crystallographic study of copper-containing nitrous oxide reductase from Pseudomonas nautica 617
    • Prudencio, M., Pereira, A., Tavares, P., Besson, S., Cabrito, I., Brown, K., Samyn, B., Devreese, B., Van Beeumen, J., Rusnak, F. et al. (2000) Purification, characterization, and preliminary crystallographic study of copper-containing nitrous oxide reductase from Pseudomonas nautica 617. Biochemistry. 39, 3899-3907
    • (2000) Biochemistry , vol.39 , pp. 3899-3907
    • Prudencio, M.1    Pereira, A.2    Tavares, P.3    Besson, S.4    Cabrito, I.5    Brown, K.6    Samyn, B.7    Devreese, B.8    Van Beeumen, J.9    Rusnak, F.10
  • 23
    • 0035977617 scopus 로고    scopus 로고
    • Characterization of the copper-sulfur chromophores in nitrous oxide reductase by resonance Raman spectroscopy: Evidence for sulfur coordination in the catalytic cluster
    • Alvarez, M. L., Ai, J., Zumft, W., Sanders-Loehr, J. and Dooley, D. M. (2001) Characterization of the copper-sulfur chromophores in nitrous oxide reductase by resonance Raman spectroscopy: evidence for sulfur coordination in the catalytic cluster. J. Am. Chem. Soc. 123, 576-587
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 576-587
    • Alvarez, M.L.1    Ai, J.2    Zumft, W.3    Sanders-Loehr, J.4    Dooley, D.M.5
  • 26
    • 0027440731 scopus 로고
    • Sequence and expression of the gene encoding the respiratory nitrous-oxide reductase from Paracoccus denitrificans
    • Hoeren, F. U., Berks, B. C., Ferguson, S. J. and McCarthy, J. E. G. (1993) Sequence and expression of the gene encoding the respiratory nitrous-oxide reductase from Paracoccus denitrificans. Eur. J. Biochem. 218, 49-57
    • (1993) Eur. J. Biochem. , vol.218 , pp. 49-57
    • Hoeren, F.U.1    Berks, B.C.2    Ferguson, S.J.3    McCarthy, J.E.G.4
  • 27
    • 0022821996 scopus 로고
    • Cytochrome c oxidase from Paracoccus denitrificans
    • Ludwig, B. (1986) Cytochrome c oxidase from Paracoccus denitrificans. Methods Enzymol. 126, 153-159
    • (1986) Methods Enzymol. , vol.126 , pp. 153-159
    • Ludwig, B.1
  • 28
    • 0348208129 scopus 로고    scopus 로고
    • Determination of absorbance coefficients for the unfolded and the native protein
    • Creighton, T. E., ed., IRL Press, Oxford, U.K.
    • Pace, N. and Schmid, F. X. (1997) Determination of absorbance coefficients for the unfolded and the native protein. In Protein Structure: A Practical Approach, 2nd edn. (Creighton, T. E., ed.), pp. 256-258, IRL Press, Oxford, U.K.
    • (1997) Protein Structure: A Practical Approach, 2nd Edn. , pp. 256-258
    • Pace, N.1    Schmid, F.X.2
  • 30
    • 0023654742 scopus 로고
    • Purification and some characteristics of nitrous oxide reductase from Paracoccus denitrificans
    • Snyder, S. W. and Holtocher, T. C. (1987) Purification and some characteristics of nitrous oxide reductase from Paracoccus denitrificans. J. Biol. Chem. 262, 6515-6525
    • (1987) J. Biol. Chem. , vol.262 , pp. 6515-6525
    • Snyder, S.W.1    Holtocher, T.C.2
  • 31
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 32
    • 0003076963 scopus 로고
    • Recent changes to the MOSFLM package for processing film and image plate data
    • Daresbury Laboratory, Warrington, U.K.
    • Leslie, A. G. W. (1992) Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4 and ESF-EAMCB Newsletter on Protein Crystallography, No. 26, Daresbury Laboratory, Warrington, U.K.
    • (1992) Joint CCP4 and ESF-EAMCB Newsletter on Protein Crystallography , vol.26
    • Leslie, A.G.W.1
  • 33
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • 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
  • 34
    • 0030880598 scopus 로고    scopus 로고
    • SHELXL: High resolution refinement
    • Sheldrick, G. M. and Schneider, T. R. (1997) SHELXL: high resolution refinement. Methods Enzymol. 276, 319-343
    • (1997) Methods Enzymol. , vol.276 , pp. 319-343
    • Sheldrick, G.M.1    Schneider, T.R.2
  • 35
    • 0033119895 scopus 로고    scopus 로고
    • Automated MAD and MIR structure solution
    • Terwilliger, T. C. and Berendzen, J. (1999) Automated MAD and MIR structure solution. Acta Crystallogr. D55, 849-861
    • (1999) Acta Crystallogr. , vol.D55 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 36
    • 0031058188 scopus 로고    scopus 로고
    • A maximum-likelihood heavy atom parameter refinement program for the MIR and MAD methods
    • de La Fortelle, E. and Bricogne, G. (1997) A maximum-likelihood heavy atom parameter refinement program for the MIR and MAD Methods. Methods Enzymol. 276, 472-494
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 37
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F1 ATPase
    • Abrahams, J. P. and Leslie, A. G. W. (1996) Methods used in the structure determination of bovine mitochondrial F1 ATPase. Acta Crystallogr. D52, 30-41
    • (1996) Acta Crystallogr. , vol.D52 , pp. 30-41
    • Abrahams, J.P.1    Leslie, A.G.W.2
  • 38
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994) AMoRe: an automated package for molecular replacement. Acta Crystallogr. A50, 157-163
    • (1994) Acta Crystallogr. , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 39
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W, and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps 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    Kjeldgaard, M.4
  • 41
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR systems: A new software suite for macromolecular structure determination
    • Bruenger, A. T. (1998) Crystallography and NMR systems: a new software suite for macromolecular structure determination. Acta Crystallogr. D54, 905-921
    • (1998) Acta Crystallogr. , vol.D54 , pp. 905-921
    • Bruenger, A.T.1
  • 42
    • 0033083840 scopus 로고    scopus 로고
    • Biochemical characterization and solution structure of nitrous oxide reductase from Alcaligenes xylosoxidans (NCIMB 11015)
    • Ferretti, S., Grossmann, J. G., Hasnain, S. S., Eady, R. R. and Smith, B. E. (1999) Biochemical characterization and solution structure of nitrous oxide reductase from Alcaligenes xylosoxidans (NCIMB 11015). Eur. J. Biochem. 259, 651-659
    • (1999) Eur. J. Biochem. , vol.259 , pp. 651-659
    • Ferretti, S.1    Grossmann, J.G.2    Hasnain, S.S.3    Eady, R.R.4    Smith, B.E.5
  • 44
    • 0034042114 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of nitrous oxide reductase from Paracoccus pantotrophus
    • Jafferiji, A., Sami, M., Nuttall, J., Ferguson, S. J., Berks, B. and Fülöp, V. (2000) Crystallization and preliminary X-ray analysis of nitrous oxide reductase from Paracoccus pantotrophus. Acta Crystallogr. D56, 653-655
    • (2000) Acta Crystallogr. , vol.D56 , pp. 653-655
    • Jafferiji, A.1    Sami, M.2    Nuttall, J.3    Ferguson, S.J.4    Berks, B.5    Fülöp, V.6
  • 46
    • 0032919371 scopus 로고    scopus 로고
    • Protein folds and families: Sequence and structure alignments
    • Holm, L. and Sander, C. (1999) Protein folds and families: sequence and structure alignments. Nucleic Acids Res. 27, 244-247
    • (1999) Nucleic Acids Res. , vol.27 , pp. 244-247
    • Holm, L.1    Sander, C.2
  • 47
    • 0242558716 scopus 로고    scopus 로고
    • β-propellers: Structural rigidity and functional diversity
    • Fülöp, V. and Jones, D. T. (1999) β-Propellers: structural rigidity and functional diversity. Curr. Opin. Struct. Biol. 9, 715-721
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 715-721
    • Fülöp, V.1    Jones, D.T.2
  • 49
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling ion biological oxidation-reduction
    • Page, C. C., Moser, C. C., Chen, X. and Dutton, P. L. (1999) Natural engineering principles of electron tunnelling ion biological oxidation-reduction. Nature (London) 402, 47-52
    • (1999) Nature (London) , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.3    Dutton, P.L.4
  • 52
    • 0026737314 scopus 로고
    • Structure of porin refined at 1.8 Å resolution
    • Weiss, M. S. and Schulz, G. E. (1992) Structure of porin refined at 1.8 Å resolution. J. Mol. Biol. 227, 493-509
    • (1992) J. Mol. Biol. , vol.227 , pp. 493-509
    • Weiss, M.S.1    Schulz, G.E.2
  • 53
    • 0002175551 scopus 로고    scopus 로고
    • Solubility of selected gases in water
    • Lide, D. R., ed., CRC Press, Boca Raton, FL
    • Gevantman, L. H. (1998) Solubility of selected gases in water. In CRC Handbook of Chemistry and Physics, 79th edn. (Lide, D. R., ed.), pp. 8-87, CRC Press, Boca Raton, FL
    • (1998) CRC Handbook of Chemistry and Physics, 79th Edn. , pp. 8-87
    • Gevantman, L.H.1
  • 55
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991) Molscript: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 56
    • 0028057108 scopus 로고
    • Raster3D Version 2.0: A program for photorealistic molecular graphics
    • Merritt, E. A. and Murphy, M. E. P. (1994) Raster3D Version 2.0: a program for photorealistic molecular graphics. Acta Crystallogr. D50, 869-873
    • (1994) Acta Crystallogr. , vol.D50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.