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Volumn 181, Issue 8, 1999, Pages 2323-2329

The blue copper-containing nitrite reductase from Alcaligenes xylosoxidans: Cloning of the nirA gene and characterization of the recombinant enzyme

Author keywords

[No Author keywords available]

Indexed keywords

NITRITE REDUCTASE;

EID: 0344573109     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.8.2323-2329.1999     Document Type: Article
Times cited : (36)

References (45)
  • 1
    • 0027437592 scopus 로고
    • Purification and characterization of the dissimilatory nitrite reductase from Alcaligenes xylosoxidans subsp. Xylosoxidans (N.C.I.M.B.): Evidence for the presence of both type 1 and type 2 copper centres
    • Abraham, Z. H. L., D. J. Lowe, and B. E. Smith. 1993. Purification and characterization of the dissimilatory nitrite reductase from Alcaligenes xylosoxidans subsp. xylosoxidans (N.C.I.M.B.): 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
  • 2
    • 0030920834 scopus 로고    scopus 로고
    • pH-dependence for binding a single nitrite ion to each type-2 copper centre in the copper-containing nitrite reductase of Alcaligenes xylosoxidans
    • Abraham, Z. H. L., B. E. Smith, B. D. Howes, D. J. Lowe, and R. R. Eady. 1997. pH-dependence for binding a single nitrite ion to each type-2 copper centre in the copper-containing nitrite reductase of Alcaligenes xylosoxidans. Biochem. J. 324:511-516.
    • (1997) Biochem. J. , vol.324 , pp. 511-516
    • Abraham, Z.H.L.1    Smith, B.E.2    Howes, B.D.3    Lowe, D.J.4    Eady, R.R.5
  • 4
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for proteins binding complex redox cofactors?
    • Berks, B. C. 1996. A common export pathway for proteins binding complex redox cofactors? Mol. Microbiol. 22:393-404.
    • (1996) Mol. Microbiol. , vol.22 , pp. 393-404
    • Berks, B.C.1
  • 5
    • 0029872903 scopus 로고    scopus 로고
    • Cloning, characterization, and expression of the nitric oxide-generating nitrite reductase and of the blue copper protein genes of Achromobacter cycloclastes
    • Chen, J.-Y., W.-C. Chang, T. Chang, W.-C. Chang, M.-Y. Liu, W. J. Payne, and J. LeGall. 1996. Cloning, characterization, and expression of the nitric oxide-generating nitrite reductase and of the blue copper protein genes of Achromobacter cycloclastes. Biochem. Biophys. Res. Commun. 219:423-428.
    • (1996) Biochem. Biophys. Res. Commun. , vol.219 , pp. 423-428
    • Chen, J.-Y.1    Chang, W.-C.2    Chang, T.3    Chang, W.-C.4    Liu, M.-Y.5    Payne, W.J.6    LeGall, J.7
  • 6
    • 0030811144 scopus 로고    scopus 로고
    • Structures of a blue copper nitrite reductase and its substrate bound complex
    • Dodd, F. E., S. S. Hasnain, Z. H. L. Abraham, R. R. Eady, B. E. Smith. 1997. Structures of a blue copper nitrite reductase and its substrate bound complex. Acta Crystallogr. D53:406-418.
    • (1997) Acta Crystallogr. , vol.D53 , pp. 406-418
    • Dodd, F.E.1    Hasnain, S.S.2    Abraham, Z.H.L.3    Eady, R.R.4    Smith, B.E.5
  • 7
    • 0032544483 scopus 로고    scopus 로고
    • X-ray structure of a blue nitrite reductase in two crystal forms. The nature of the copper sites, mode of substrate binding and recognition by redox partner
    • Dodd, F. E., J. Van Beeumen, R. R. Eady, and S. S. Hasnain. 1998. X-ray structure of a blue nitrite reductase in two crystal forms. The nature of the copper sites, mode of substrate binding and recognition by redox partner. J. Mol. Biol. 282:369-382.
    • (1998) J. Mol. Biol. , vol.282 , pp. 369-382
    • Dodd, F.E.1    Van Beeumen, J.2    Eady, R.R.3    Hasnain, S.S.4
  • 8
    • 0345485983 scopus 로고    scopus 로고
    • Unpublished data
    • Eady, R. Unpublished data.
    • Eady, R.1
  • 9
    • 0032475972 scopus 로고    scopus 로고
    • The intramolecular electron transfer between copper sites of nitrite reductase: A comparison with ascorbate oxidase
    • Farver, O., R. R. Eady, Z. H. L. Abraham, and I. Pecht. 1998. The intramolecular electron transfer between copper sites of nitrite reductase: a comparison with ascorbate oxidase. FEBS Lett. 436:239-242.
    • (1998) FEBS Lett. , vol.436 , pp. 239-242
    • Farver, O.1    Eady, R.R.2    Abraham, Z.H.L.3    Pecht, I.4
  • 10
    • 0025748667 scopus 로고
    • Amino acid sequence of nitrite reductase: A copper protein from Achromobacter cycloclastes
    • Fenderson, F. F., S. Kumar, E. T. Adman, M.-Y. Liu, W. J. Payne, and J. Legall. 1991. Amino acid sequence of nitrite reductase: a copper protein from Achromobacter cycloclastes. Biochemistry 30:7180-7187.
    • (1991) Biochemistry , vol.30 , pp. 7180-7187
    • Fenderson, F.F.1    Kumar, S.2    Adman, E.T.3    Liu, M.-Y.4    Payne, W.J.5    Legall, J.6
  • 12
    • 0026353602 scopus 로고
    • The 2.3 angstrom X-ray structure of nitrite reductase from Achromobacter cycloclastes
    • Godden, J. W., S. Turley, D. C. Teller, E. T. Adman, M. Y. Liu, W. J. Payne, and J. LeGall. 1991. The 2.3 angstrom 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
  • 13
    • 0027223884 scopus 로고
    • X-ray scattering using synchrotron radiation shows nitrite reductase from Achromobacter xylosoxidans to be a trimer in solution
    • Grossmann, J. G., Z. H. L. Abraham, E. T. Adman, M. Neu, R. R. Eady, B. E. Smith, and S. S. Hasnain. 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    M, N.4    Eady, R.R.5    Smith, B.E.6    Hasnain, S.S.7
  • 14
    • 0345485970 scopus 로고    scopus 로고
    • Personal communication
    • Hasnain, S. S. Personal communication.
    • Hasnain, S.S.1
  • 15
    • 0028267847 scopus 로고
    • EPR and electron nuclear double resonance (ENDOR) studies show nitrite binding to the type 2 copper centers of the dissimilatory nitrite reductase of Akaligenes xylosoxidans (NCIMB 11015)
    • Howes, B. D., Z. H. L. Abraham, D. J. Lowe, T. Brüser, R. R. Eady, and B. E. Smith. 1994. EPR and electron nuclear double resonance (ENDOR) studies show nitrite binding to the type 2 copper centers of the dissimilatory nitrite reductase of Akaligenes xylosoxidans (NCIMB 11015). Biochemistry 33:3171-3177.
    • (1994) Biochemistry , vol.33 , pp. 3171-3177
    • Howes, B.D.1    Abraham, Z.H.L.2    Lowe, D.J.3    Brüser, T.4    Eady, R.R.5    Smith, B.E.6
  • 16
    • 0031786665 scopus 로고    scopus 로고
    • Type 1 Cu structure of blue nitrite reductase from Alcaligenes xylosoxidans GIFU 1051 at 2.05 Å resolution: Comparison of blue and green nitrite reductase
    • Inoue, T., M. Gotowda, S. Deeliger, K. Kataoka, K. Yamaguchi, S. Suzuki, H. Watanabe, M. Gohow, and Y. Kai. 1998. Type 1 Cu structure of blue nitrite reductase from Alcaligenes xylosoxidans GIFU 1051 at 2.05 Å resolution: comparison of blue and green nitrite reductase. J. Biochem. 124:876-879.
    • (1998) J. Biochem. , vol.124 , pp. 876-879
    • Inoue, T.1    Gotowda, M.2    Deeliger, S.3    Kataoka, K.4    Yamaguchi, K.5    Suzuki, S.6    Watanabe, H.7    Gohow, M.8    Kai, Y.9
  • 17
    • 0028298314 scopus 로고
    • X-ray structure and site-directed mutagenesis of a nitrite reductase from Alcaligenes faecalis s-6: Roles of two copper atoms in nitrite reduction
    • Kukimoto, M., M. Nishiyama, M. E. P. Murphy, S. Turley, E. T. Adman, S. Horinouchi, and T. Beppu. 1994. X-ray structure and site-directed mutagenesis of a nitrite reductase from Alcaligenes faecalis S-6: roles of two 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
  • 18
    • 0029794252 scopus 로고    scopus 로고
    • Electronic structures of the perturbed blue copper site in nitrite reductase: Spectroscopic properties, bonding, and implications for the entatic/rack state
    • LaCroix, L. B., S. E. Shadle, Y. Wang, B. A. Averill, B. Hedman, K. O. Hodgson, and E. I. Solomon. 1996. Electronic structures 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.3    Averill, B.A.4    Hedman, B.5    Hodgson, K.O.6    Solomon, E.I.7
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0026701748 scopus 로고
    • Evidence that the type 2 copper centres are the site of nitrite reduction by Achromobacter cycloclastes nitrite reductase
    • Libby, E., and B. A. Averill. 1992. Evidence that the type 2 copper centres are the site of nitrite reduction by Achromobacter cycloclastes nitrite reductase. Biochem. Biophys. Res. Commun. 187:1529-1535.
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 1529-1535
    • Libby, E.1    Averill, B.A.2
  • 22
    • 0017888713 scopus 로고
    • Electron paramagnetic resonance spectroscopy: Computer simulation of spectra from frozen aqueous samples
    • Lowe, D. J. 1978. Electron paramagnetic resonance spectroscopy: computer simulation of spectra from frozen aqueous samples. Biochem. J. 171:649-651.
    • (1978) Biochem. J. , vol.171 , pp. 649-651
    • Lowe, D.J.1
  • 24
    • 0027229994 scopus 로고
    • Cloning and characterization of a nitrite reductase gene from Alcaligenes faecalis and its expression in Escherichia coli
    • Nishiyama, M., J. Suzuki, M. Kukimoto, T. Ohnuki, S. Horinouchi, and T. Beppu. 1993. Cloning and characterization of a nitrite reductase gene from Alcaligenes faecalis and its expression in Escherichia coli. J. Gen. Microbiol. 139:725-733.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 725-733
    • Nishiyama, M.1    Suzuki, J.2    Kukimoto, M.3    Ohnuki, T.4    Horinouchi, S.5    Beppu, T.6
  • 25
    • 0032574836 scopus 로고    scopus 로고
    • Spectroscopic, kinetic, and electrochemical characterization of heterogeneously expressed wild-type and mutant forms of copper-containing nitrite reductase from Rhodobacter sphaeroides 2.4.3
    • Olesen, K., A. Veselov, Y. Zhao, Y. Wang, B. Danner, C. P. Scoles, and J. P. Shapleigh. 1998. Spectroscopic, kinetic, and electrochemical characterization of heterogeneously expressed wild-type and mutant forms of copper-containing nitrite reductase from Rhodobacter sphaeroides 2.4.3. Biochemistry 37:6086-6094.
    • (1998) Biochemistry , vol.37 , pp. 6086-6094
    • Olesen, K.1    Veselov, A.2    Zhao, Y.3    Wang, Y.4    Danner, B.5    Scoles, C.P.6    Shapleigh, J.P.7
  • 26
    • 0015523247 scopus 로고
    • Mechanism of assembly of the outer membrane of Salmonella typhimurium
    • Osborn, M. J., J. E. Gander, and E. Parisi. 1972. Mechanism of assembly of the outer membrane of Salmonella typhimurium. J. Biol. Chem. 247:3973-3986.
    • (1972) J. Biol. Chem. , vol.247 , pp. 3973-3986
    • Osborn, M.J.1    Gander, J.E.2    Parisi, E.3
  • 27
    • 1542563726 scopus 로고    scopus 로고
    • Partial inverse PCR: A technique for cloning flanking sequences
    • Pang, K. M., and D. A. Knecht. 1997. Partial inverse PCR: a technique for cloning flanking sequences. BioTechniques 22:1046-1048.
    • (1997) BioTechniques , vol.22 , pp. 1046-1048
    • Pang, K.M.1    Knecht, D.A.2
  • 30
    • 0032472381 scopus 로고    scopus 로고
    • A novel sec-independent periplasmic protein translocation pathway in Escherichia coli
    • Santini, C.-L., B. Ize, A. Chanal, M. Müller, G. Giordano, and L.-F. Wu. 1998. A novel Sec-independent periplasmic protein translocation pathway in Escherichia coli. EMBO J. 17:101-112.
    • (1998) EMBO J , vol.17 , pp. 101-112
    • Santini, C.-L.1    Ize, B.2    Chanal, A.3    Müller, M.4    Giordano, G.5    Wu, L.-F.6
  • 31
    • 0032127435 scopus 로고    scopus 로고
    • Overlapping functions of components of a bacterial Sec-independent protein export pathway
    • Sargent, F., E. G. Bogsch, N. R. Stanley, M. Wexler, C. Robinson, B. C. Berks, and T. Palmer. 1998. Overlapping functions of components of a bacterial Sec-independent protein export pathway. EMBO J. 17:3640-3650.
    • (1998) EMBO J. , vol.17 , pp. 3640-3650
    • Sargent, F.1    Bogsch, E.G.2    Stanley, N.R.3    Wexler, M.4    Robinson, C.5    Berks, B.C.6    Palmer, T.7
  • 32
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct high-level expression of cloned genes
    • Studier, F. W., and B. A. Moffat. 1986. Use of bacteriophage T7 RNA polymerase to direct high-level expression of cloned genes. J. Mol. Biol. 189:113-130.
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffat, B.A.2
  • 34
    • 85018193510 scopus 로고
    • Pulse radiolysis studies on nitrite reductase from Achromobacter cycloclastes IAM 1013: Evidence for intramolecular electron transfer from type 1 Cu to type 2 Cu
    • Suzuki, S., T. Kohzuma, S. Deeliger, K. Yamaguchi, N. Nakmura, S. Shidara, K. Kobayashi, and S. Tagawa. 1994. Pulse radiolysis studies on nitrite reductase from Achromobacter cycloclastes IAM 1013: evidence for intramolecular electron transfer from type 1 Cu to type 2 Cu. J. Am. Chem. Soc. 116:11145-11146.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 11145-11146
    • Suzuki, S.1    Kohzuma, T.2    Deeliger, S.3    Yamaguchi, K.4    Nakmura, N.5    Shidara, S.6    Kobayashi, K.7    Tagawa, S.8
  • 35
    • 0021919826 scopus 로고
    • A bacteriophage T7 polymerase/promoter system for controlled exclusive expression of specific genes
    • Tabor, S., and C. C. Richardson. 1985. A bacteriophage T7 polymerase/promoter system for controlled exclusive expression of specific genes. Proc. Natl. Acad. Sci. USA 82:1074-1078.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 1074-1078
    • Tabor, S.1    Richardson, C.C.2
  • 36
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 37
    • 0029802510 scopus 로고    scopus 로고
    • Characterization of the gene encoding nitrite reductase and the physiological consequences of its expression in the nondenitrifying Rhizobium "hedysari" strain HCNT1
    • Toffanin, A., Q. Wu, M. Maskus, S. Casella, H. D. Abruña, and J. P. Shapleigh. 1996. Characterization of the gene encoding nitrite reductase and the physiological consequences of its expression in the nondenitrifying Rhizobium "hedysari" strain HCNT1. Appl. Environ. Microbiol. 62:4019-4025
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 4019-4025
    • Toffanin, A.1    Wu, Q.2    Maskus, M.3    Casella, S.4    Abruña, H.D.5    Shapleigh, J.P.6
  • 38
    • 0031047127 scopus 로고    scopus 로고
    • Characterization and regulation of the gene encoding nitrite reductase in rhodobacter sphaeroides 2.4.3
    • Tosques, I. E., A. V. Kwiatkowski, J. Shi, and J. P. Shapleigh. 1997. Characterization and regulation of the gene encoding nitrite reductase in Rhodobacter sphaeroides 2.4.3. J. Bacteriol. 179:1090-1095.
    • (1997) J. Bacteriol. , vol.179 , pp. 1090-1095
    • Tosques, I.E.1    Kwiatkowski, A.V.2    J, S.3    Shapleigh, J.P.4
  • 39
    • 0344623788 scopus 로고    scopus 로고
    • Personal communication
    • Van Beeumen, J. J. Personal communication.
    • Van Beeumen, J.J.1
  • 40
    • 0032577905 scopus 로고    scopus 로고
    • The covalent structure of the blue copper-containing nitrite reductase from Achromobacter xylosoxidans
    • Vandenberghe, I. H. M., T. E. Meyer, M. A. Cusanovich, and J. J. Van Beeumen. 1998. The covalent structure of the blue copper-containing nitrite reductase from Achromobacter xylosoxidans. Biochem. Biophys. Res. Commun. 247:734-740.
    • (1998) Biochem. Biophys. Res. Commun. , vol.247 , pp. 734-740
    • Vandenberghe, I.H.M.1    Meyer, T.E.2    Cusanovich, M.A.3    Van Beeumen, J.J.4
  • 41
    • 0032574685 scopus 로고    scopus 로고
    • Electronic structural information from Q-band ENDOR on the type 1 and type 2 copper liganding environment in wild-type and mutant forms of copper-containing nitrite reductase
    • Veselov, A., K. Olesen, A. Sienkiewicz, J. P. Shapleigh, and C. P. Scholes. 1998. Electronic structural information from Q-band ENDOR on the type 1 and type 2 copper liganding environment in wild-type and mutant forms of copper-containing nitrite reductase. Biochemistry 37:6095-6105.
    • (1998) Biochemistry , vol.37 , pp. 6095-6105
    • Veselov, A.1    Olesen, K.2    Sienkiewicz, A.3    Shapleigh, J.P.4    Scholes, C.P.5
  • 42
    • 0032478550 scopus 로고    scopus 로고
    • A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins
    • Weiner, J. H., P. T. Bilous, G. M. Shaw, S. P. Lubitz, L. Frost, G. H. Thomas, J. A. Cole, and R. J. Turner. 1998. A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins. Cell 93: 93-101.
    • (1998) Cell , vol.93 , pp. 93-101
    • Weiner, J.H.1    Bilous, P.T.2    Shaw, G.M.3    Lubitz, S.P.4    Frost, L.5    Thomas, G.H.6    Cole, J.A.7    Turner, R.J.8
  • 43
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp19 and pUC19 vectors
    • Vanish-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp19 and pUC19 vectors. Gene 33:103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Vanish-Perron, C.1    Vieira, J.2    Messing, J.3
  • 44
    • 0027531490 scopus 로고
    • Characterization of the structural gene encoding a copper-containing nitrite reductase and homology of this gene to DNA of other denitrifiers
    • Ye, R. W., M. R. Fries, S. G. Bezborodnikov, B. A. Averill, and J. M. Tiedje. 1993. Characterization of the structural gene encoding a copper-containing nitrite reductase and homology of this gene to DNA of other denitrifiers. Appl. Environ. Microbiol. 59:250-254.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 250-254
    • Ye, R.W.1    Fries, M.R.2    Bezborodnikov, S.G.3    Averill, B.A.4    Tiedje, J.M.5
  • 45
    • 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


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