메뉴 건너뛰기




Volumn 282, Issue 2, 1998, Pages 369-382

X-ray structure of a blue-copper nitrite reductase in two crystal forms. The nature of the copper sites, mode of substrate binding and recognition by redox partner

Author keywords

Carbonic anhydrase; Catalysis; Denitrification; Electron transfer; Superoxide dismutase

Indexed keywords

AZURIN; CARBONATE DEHYDRATASE; COPPER; NITRITE REDUCTASE; SUPEROXIDE DISMUTASE;

EID: 0032544483     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2007     Document Type: Article
Times cited : (130)

References (30)
  • 1
    • 0027437592 scopus 로고
    • Purification and characterization of dissimilatory nitrite reductase from Alcaligenes xylosoxidans subsp. xylosoxidans (NCIMB 11015): Evidence for the presence of both type 1 and type 2 copper centres
    • Abraham, Z. H. L., Lowe, D. J. & Smith, B. E. (1993). Purification and characterization of dissimilatory nitrite reductase from Alcaligenes xylosoxidans subsp. xylosoxidans (NCIMB 11015): evidence for the presence of both type 1 and type 2 copper centres. Biochem. J. 295, 587-593.
    • (1993) Biochem. J. , vol.295 , pp. 587-593
    • Abraham, Z.H.L.1    Lowe, D.J.2    Smith, B.E.3
  • 3
    • 0024293340 scopus 로고
    • Structure of azurin from Alcaligenes denitrificans. Refinement at 1.8 Å resolution and comparison of the two crystallographically independent molecules
    • Baker, E. N. (1988). Structure of azurin from Alcaligenes denitrificans. Refinement at 1.8 Å resolution and comparison of the two crystallographically independent molecules. J. Mol. Biol. 203, 1071-1075.
    • (1988) J. Mol. Biol. , vol.203 , pp. 1071-1075
    • Baker, E.N.1
  • 6
    • 0029187321 scopus 로고
    • Structure of a new azurin from the denitrifying bacterium Alcaligenes xylosoxidans at high resolution
    • Dodd, F. E., Hasnain, S. S., Abraham, Z. H. L., Eady, R. R. & Smith, B. E. (1995). Structure of a new azurin from the denitrifying bacterium Alcaligenes xylosoxidans at high resolution. Acta Crystallog. sect. D, 51, 1052-1064.
    • (1995) Acta Crystallog. Sect. D , vol.51 , pp. 1052-1064
    • Dodd, F.E.1    Hasnain, S.S.2    Abraham, Z.H.L.3    Eady, R.R.4    Smith, B.E.5
  • 8
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4, (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D, 50, 760-763.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 9
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R. A. & Huber, R. (1991). Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallog. sect. A, 47, 392-400.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 11
    • 0026353602 scopus 로고
    • The 2.3 Å X-ray structure of nitrite reductase from Achromobacter cycloclastes
    • Godden, J. W., Turley, S., Teller, D. C., Adman, E. T., Liu, M. Y., Payne, W. J. & LeGall, J. (1991). The 2.3 Å X-ray structure of nitrite reductase from Achromobacter cycloclastes. Science, 253, 438-442.
    • (1991) Science , vol.253 , pp. 438-442
    • Godden, J.W.1    Turley, S.2    Teller, D.C.3    Adman, E.T.4    Liu, M.Y.5    Payne, W.J.6    LeGall, J.7
  • 12
    • 0027223884 scopus 로고
    • X-ray scattering using synchrotron radiation shows nitrite reductase from Achromobacter xylosoxidans to be a trimer in solution
    • Grossmann, J. G., Abraham, Z. H. L., Adman, E. T., Neu, M., Eady, R. R., Smith, B. E. & Hasnain, S. S. (1993). X-ray scattering using synchrotron radiation shows nitrite reductase from Achromobacter xylosoxidans to be a trimer in solution. Biochemistry, 32, 7360-7366.
    • (1993) Biochemistry , vol.32 , pp. 7360-7366
    • Grossmann, J.G.1    Abraham, Z.H.L.2    Adman, E.T.3    Neu, M.4    Eady, R.R.5    Smith, B.E.6    Hasnain, S.S.7
  • 13
    • 0032128139 scopus 로고    scopus 로고
    • Structure determination of a 16.8 kDa copper protein at 2.1 Å resolution using anomalous scattering data and direct methods
    • Harvey, I., Mao, Q., Duke, E. M. H., Ingledew, W. J. & Hasnain, S. S. (1998). Structure determination of a 16.8 kDa copper protein at 2.1 Å resolution using anomalous scattering data and direct methods. Acta Crystallog. sect D, 54, 629-635.
    • (1998) Acta Crystallog. Sect D , vol.54 , pp. 629-635
    • Harvey, I.1    Mao, Q.2    Duke, E.M.H.3    Ingledew, W.J.4    Hasnain, S.S.5
  • 14
    • 0026605537 scopus 로고
    • CLUSTAL-V: Improved software for multiple sequence alignment
    • Higgins, D. G., Bleasby, A. J. & Fuchs, R. (1992). CLUSTAL-V: improved software for multiple sequence alignment. CABIOS, 8, 189-191.
    • (1992) CABIOS , vol.8 , pp. 189-191
    • Higgins, D.G.1    Bleasby, A.J.2    Fuchs, R.3
  • 15
    • 0015327555 scopus 로고
    • A nitrite reductase from Achromobacter cycloclastes
    • Iwasaki, H. & Matsubara, T. (1972). A nitrite reductase from Achromobacter cycloclastes. J. Biochem. 71, 645-652.
    • (1972) J. Biochem. , vol.71 , pp. 645-652
    • Iwasaki, H.1    Matsubara, T.2
  • 16
    • 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. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A, 47, 110-119.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 17
    • 0029874435 scopus 로고    scopus 로고
    • A left handed beta helix revealed by the crystal-structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila
    • Kisker, C., Schindelin, H., Alber, B. E., Ferry, J. G. & Rees, D. C. (1996). A left handed beta helix revealed by the crystal-structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila. EMBO J. 15, 2323-2330.
    • (1996) EMBO J. , vol.15 , pp. 2323-2330
    • Kisker, C.1    Schindelin, H.2    Alber, B.E.3    Ferry, J.G.4    Rees, D.C.5
  • 18
    • 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. Crystallog. 24, 946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 19
    • 0028298314 scopus 로고
    • X-ray structure and site-directed mutagenesis of a nitrite reductase from Alcaligenes faecalis S-6-roles of 2 copper atoms in nitrite reduction
    • Kukimoto, M., Nishiyama, M., Murphy, M. E. P., Turley, S., Adman, E. T., Horinouchi, S. & Beppu, T. (1994). X-ray structure and site-directed mutagenesis of a nitrite reductase from Alcaligenes faecalis S-6-roles of 2 copper atoms in nitrite reduction. Biochemistry, 33, 5246-5252.
    • (1994) Biochemistry , vol.33 , pp. 5246-5252
    • Kukimoto, M.1    Nishiyama, M.2    Murphy, M.E.P.3    Turley, S.4    Adman, E.T.5    Horinouchi, S.6    Beppu, T.7
  • 20
    • 0028958832 scopus 로고
    • Identification of interaction site of pseudoazurin with its redox partner, copper containing nitrite reductase from Alcaligenes faecalis S-6
    • Kukimoto, M., Nishiyama, M., Ohnuki, T., Turley, S., Adman, E. T., Horinouchi, S. & Beppu, T. (1995). Identification of interaction site of pseudoazurin with its redox partner, copper containing nitrite reductase from Alcaligenes faecalis S-6. Protein Eng. 8, 153-158.
    • (1995) Protein Eng. , vol.8 , pp. 153-158
    • Kukimoto, M.1    Nishiyama, M.2    Ohnuki, T.3    Turley, S.4    Adman, E.T.5    Horinouchi, S.6    Beppu, T.7
  • 21
    • 0029794252 scopus 로고    scopus 로고
    • Electronic structure of the perturbed blue copper site in nitrite reductase spectroscopic properties, bonding, and implications for the entatic/rack state
    • LaCroix, L. B., Shadle, S. E., Wang, Y. N., Averill, B. A., Hedman, B., Hodgson, K. O. & Solomon, E. I. (1996). Electronic structure of the perturbed blue copper site in nitrite reductase spectroscopic properties, bonding, and implications for the entatic/rack state. J. Am. Chem. Soc. 188, 7755-7768.
    • (1996) J. Am. Chem. Soc. , vol.188 , pp. 7755-7768
    • Lacroix, L.B.1    Shadle, S.E.2    Wang, Y.N.3    Averill, B.A.4    Hedman, B.5    Hodgson, K.O.6    Solomon, E.I.7
  • 22
    • 0031569326 scopus 로고    scopus 로고
    • A critical assessment of the evidence from XAFS and crystallography for the breakage of the imidazolate bridge during catalysis in CuZn superoxide dismutase
    • Murphy, L. M., Strange, R. W. & Hasnain, S. S. (1997). A critical assessment of the evidence from XAFS and crystallography for the breakage of the imidazolate bridge during catalysis in CuZn superoxide dismutase. Structure, 5, 371-379.
    • (1997) Structure , vol.5 , pp. 371-379
    • Murphy, L.M.1    Strange, R.W.2    Hasnain, S.S.3
  • 24
    • 0025953438 scopus 로고
    • Crystal structure analysis of oxidised Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0
    • Nar, H., Messerschmidt, A., Huber, R., van de Kamp, M. & Canters, G. W. (1991). Crystal structure analysis of oxidised Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0. J. Mol. Biol. 221, 765-772.
    • (1991) J. Mol. Biol. , vol.221 , pp. 765-772
    • Nar, H.1    Messerschmidt, A.2    Huber, R.3    Van De Kamp, M.4    Canters, G.W.5
  • 25
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994). AMoRe: an automated package for molecular replacement. Acta. Crystallog. sect. A, 50, 157-163.
    • (1994) Acta. Crystallog. Sect. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 27
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • (Carter, C. W., Jr & Sweet, R. M., eds), Academic Press
    • Otwinowski, Z. & Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. In Methods in Enzymology (Carter, C. W., Jr & Sweet, R. M., eds), vol. 276, pp. 307-326, Academic Press.
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 30
    • 0026667697 scopus 로고
    • Characterization of Tn5 mutants deficient in dissimilatory nitrite reductase in Pseudomonas sp. strain G-179, which contain a copper nitrite reductase
    • Ye, R. W., Averill, B. A. & Tiedje, J. M. (1992). Characterization of Tn5 mutants deficient in dissimilatory nitrite reductase in Pseudomonas sp. strain G-179, which contain a copper nitrite reductase. J. Bacteriol. 174, 6653-6658.
    • (1992) J. Bacteriol. , vol.174 , pp. 6653-6658
    • Ye, R.W.1    Averill, B.A.2    Tiedje, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.