High resolution structural studies of mutants provide insights into catalysis and electron transfer processes in copper nitrite reductase

Journal of Molecular Biology

Volumn 350, Issue 2, 2005, Pages 300-309

  Hough, Michael A ^a   Ellis, Mark J ^a   Antonyuk, Svetlana ^a   Strange, Richard W ^a   Sawers, Gary ^b   Eady, Robert R ^a   Hasnain, S Samar ^a  

^a DARESBURY LABORATORY   (United Kingdom)

^b JOHN INNES CENTRE   (United Kingdom)

Author keywords

Alcaligenes xylosoxidans; Axial ligand; Catalysis; Denitrification; Nitrite reductase; Redox potential

Indexed keywords

AZURIN; LEUCINE; METHIONINE; NITRITE; NITRITE REDUCTASE;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ELECTRON; ELECTRON TRANSPORT; ENZYME INACTIVATION; MUTANT; MUTATION; OXIDATION REDUCTION POTENTIAL; PRIORITY JOURNAL; STRUCTURE ANALYSIS;

ACHROMOBACTER XYLOSOXIDANS;

EID: 20444381694     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.04.006     Document Type: Article

References (30)

1. W.G. Zumft Cell biology and molecular basis of denitrification Microb. Mol. Biol. Rev. 61 1997 533 616
2. R.R. Eady, and S.S. Hasnain Denitrification Comp. Coord. Chem. 8 2003 759 786
3. M. Kukimoto, M. Nishiyama, M.E.P. Murphy, S. Turley, E.T. Adman, S. Horinouchi, and T.T. Beppu 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 1994 5246 5252
4. R.W. Strange, F.E. Dodd, Z.H.L. Abraham, J.G. Grossmann, T. Bruser, and R.R. Eady The substrate binding site in Cu nitrite reductase and its similarity to Zn carbonic anhydrase Nature Struct. Biol. 2 1995 287 292
5. R.W. Strange, L.M. Murphy, F.E. Dodd, Z.H.L. Abraham, R.R. Eady, B.E. Smith, and S.S. Hasnain Structural and kinetic evidence for an ordered mechanism of copper nitrite reductase J. Mol. Biol. 287 1999 1001 1009
6. M. Prudencio, G. Sawers, S.A. Fairhurst, F.K. Yousafzai, and R.R. Eady Alcaligenes xylosoxidans dissimilatory nitrite reductase: alanine substitution of the surface-exposed histidine 139 ligand of the type 1 copper center prevents electron transfer to the catalytic center Biochemistry 41 2002 3430 3438
7. K. Kataoka, K. Yamaguchi, S. Sakai, K. Takagi, and S. Suzuki Characterization and function of Met150Gln mutant of copper-containing nitrite reductase from Achromobacter cycloclastes IAM1013 Biochem. Biophys. Res. Commun. 303 2003 519 524
8. M.E.P. Murphy, S. Turley, M. Kukimoto, M. Nishiyama, S. Horinouchi, and H. Sasaki Structure of Alcaligenes-fecaelis nitrite reductase and a copper site mutant, M150E, that contains zinc Biochemistry 34 1995 12107 12117
9. Z.H.L. Abraham, B.E. Smith, B.D. Howes, D.J. Lowe, and R.R. Eady 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 1997 511 516
10. T. Kakutani, H. Watanabe, K. Arima, and T. Beppu Purification and properties of a copper-containing nitrite reductase from a denitrifying bacterium, Alcaligenes faecalis S-6 J. Biochem.-Tokyo 89 1981 453 461
11. J.F. Hall, L.D. Kanbi, R.W. Strange, and S.S. Hasnain Role of the axial ligand in type 1 Cu centers studied by point mutations of Met148 in rusticyanin Biochemistry 38 1999 12675 12680
12. L.D. Kanbi, S. Antonyuk, M.A. Hough, J.F. Hall, F.E. Dodd, and S.S. Hasnain Crystal structures of the Met148Leu and Ser86Asp mutants of rusticyanin from Thiobacillus ferrooxidans: insights into the structural relationship with the cupredoxins and the multi copper proteins J. Mol. Biol. 320 2002 263 275
13. V. Ducros, A.M. Brzozowski, K.S. Wilson, S.H. Brown, P. Ostergaard, and P. Schneider Crystal structure of the type-2 Cu depleted laccase from Coprinus cinereus at 2.2 angstrom resolution Nature Struct. Biol. 5 1988 310 316
14. I. Zaitseva, V. Zaitsev, G. Card, K. Moshkov, B. Bax, A. Ralph, and P. Lindley The X-ray structure of human serum ceruloplasmin at 3.1 angstrom: nature of the copper centres J. Biol. Inorg. Chem. 1 1996 15 23
15. M.A. Hough, J.F. Hall, L.D. Kanbi, and S.S. Hasnain Structure of the M148Q mutant of rusticyanin at 1.5 angstrom: a model for the copper site of stellacyanin Acta Crystallog. sect. D 57 2001 355 360
16. P.J. Hart, A.M. Nersissian, R.G. Herrmann, R.M. Nalbandyan, J.S. Valentine, and D. Eisenberg A missing link in cupredoxins: crystal structure of cucumber stellacyanin at 1.6 angstrom resolution Protein Sci. 5 1996 2175 2183
17. O. Farver, R.R. Eady, Z.H.L. Abraham, and I. Pecht The intramolecular electron transfer between copper sites of nitrite reductase: a comparison with ascorbate oxidase FEBS Letters 436 1998 239 242
18. L.M. Murphy, F.E. Dodd, F.K. Yousafzai, R.R. Eady, and S.S. Hasnain Electron donation between copper containing nitrite reductases and cupredoxins: the nature of protein-protein interaction in complex formation J. Mol. Biol. 315 2002 859 871
19. S. Suzuki, T. Kohzuma, Deligeer, K. Yamaguchi, N. Nakamura, and S. Shidara 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 1994 11145 11146
20. M.J. Ellis, M. Prudencio, F.E. Dodd, R.W. Strange, G. Sawers, R.R. Eady, and S.S. Hasnain Biochemical and crystallographic studies of the Met144Ala, Asp92Asn and His254Phe mutants of the nitrite reductase from Alcaligenes xylosoxidans provide insight into the enzyme mechanism J. Mol. Biol. 316 2002 51 64
21. L. Basumallick, R.K. Szilagyi, Y.W. Zhao, J.P. Shapleigh, C.P. Scholes, and E.I. Solomon Spectroscopic studies of the Met182Thr mutant of nitrite reductase: role of the axial ligand in the geometric and electronic structure of blue and green copper sites J. Am. Chem. Soc. 125 2003 14784 14792
22. F. Sanger, S. Nicklen, and A.R. Coulson DNA sequencing with chain-terminating inhibitors Proc. Natl Acad. Sci. USA 74 1977 5463 5467
23. Z.H.L. Abraham, D.J. Lowe, and B.E. Smith Purification and characterization of the dissimilatory nitrite reductase from Alcaligenes xylosoxidans sub xylosoxidans (NCIMB 11015): evidence for the presence of both type 1 and type 2 copper centres Biochem. J. 285 1993 587 593
24. Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1993 307 326
25. J. Navaza AMoRe: an automated package for molecular replacement Acta Crystallog. sect. A 50 1994 157 163
26. G.N. Murshudov, A.A. Vagin, and E.J. Dodson Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallog. sect. D 53 1997 240 255
27. G.M. Sheldrick, and T.R. Schneider SHELXL: high-resolution refinement Methods Enzymol. 277 1997 319 343
28. A. Vagin, and A.J. Teplyakov MOLREP: an automated program for molecular replacement Appl. Crystallog. 30 1997 1022 1025
29. F.C. Bernstein, T.F. Koetzle, G.J.B. Williams, F.M. Meyer Jr, M.D. Brice, and J.R. Rogers Protein Data Bank: computer based archival file for macromolecular structures J. Mol. Biol. 112 1977 535 542
30. M.J. Ellis, F.E. Dodd, G. Sawers, R.R. Eady, and S.S. Hasnain Atomic resolution structures of native copper nitrite reductase from Alcaligenes xylosoxidans and the active site mutant Asp92Glu J. Mol. Biol. 328 2003 429 438