Insight into Catalysis of Nitrous Oxide Reductase from High-resolution Structures of Resting and Inhibitor-bound Enzyme from Achromobacter cycloclastes

Journal of Molecular Biology

Volumn 362, Issue 1, 2006, Pages 55-65

  Paraskevopoulos, Konstantinos ^a,b   Antonyuk, Svetlana V ^b   Sawers, R Gary ^c   Eady, Robert R ^b   Hasnain, S Samar ^a,b  

^a LIVERPOOL JOHN MOORES UNIVERSITY   (United Kingdom)

^b DARESBURY LABORATORY   (United Kingdom)

^c MAX PLANCK INSTITUTE FOR TERRESTRIAL MICROBIOLOGY   (Germany)

Author keywords

catalysis; copper chemistry; denitrification; electron gating; nitrous oxide binding

Indexed keywords

COPPER; NITROGEN; NITROUS OXIDE REDUCTASE; OXYGEN; SODIUM IODIDE; WATER;

ACHROMOBACTER CYCLOCLASTES; ARTICLE; BIOLOGY; CATALYSIS; CHEMISTRY; CRYSTAL STRUCTURE; ENZYME STRUCTURE; LIGATION; NONHUMAN; PRIORITY JOURNAL; SPECTROSCOPY;

ACHROMOBACTER CYCLOCLASTES;

EID: 33747351535     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.06.064     Document Type: Article

References (31)

1. 2O) reductase. J. Biol. Chem. 275 (2000) 41133-41136
2. Z cluster of nitrous oxide reductase. J. Am. Chem. Soc. 128 (2006) 278-290
3. Zumft W.G. Cell biology and molecular basis of denitrification. Microbiol. Mol. Biol. Rev. 61 (1997) 533-616
4. Eady R.R., and Hasnain S.S. Denitrification. Compr. Coord. Chem. 8 (2003) 759-786
5. Coyle C.L., Zumft W.G., Kroneck P.M., Korner H., and Jakob W. Nitrous oxide reductase from denitrifying Pseudomonas perfectomarina. Purification and properties of a novel multicopper enzyme. Eur. J. Biochem. 153 (1985) 459-467
6. Kroneck P.M., Antholine W.A., Riester J., and Zumft W.G. The cupric site in nitrous oxide reductase contains a mixed-valence [Cu(II),Cu(I)] binuclear center: a multifrequency electron paramagnetic resonance investigation. FEBS Letters 242 (1988) 70-74
7. Haltia T., Brown K., Tegoni M., Cambillau C., Saraste M., and Djinovic-Carugo M.K. Crystal Structure of nitrous oxide reductase from Paracoccus denitrificans at 1.6 Å resolution. Bioch. J. 369 (2003) 77-88
8. Prudencio M., Pereira A.S., Tavares P., Besson S., Cabrito I., Brown K., et al. Purification, characterization, and preliminary crystallographic study of copper-containing nitrous oxide reductase from Pseudomonas nautica 617. Biochemistry 39 (2000) 3899-3907
9. Brown K., Tegoni M., Prudencio M., Pereira A.S., Besson S., Moura J.J., et al. A novel type of catalytic copper cluster in nitrous oxide reductase. Nature Struct. Biol. 7 (2000) 191-195
10. Iwata S., Ostermeier C., Ludwig B., and Michel H. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376 (1995) 660-669
11. Z cluster in nitrous oxide reductase. J. Am. Chem. Soc. 125 (2003) 15708-15709
12. Z cluster active site. Angew. Chem. Int. Ed. 43 (2004) 4132-4140
13. 2O reductase: Molecular insight into the catalytic mechanism. J. Am. Chem. Soc. 124 (2002) 10497-10507
14. 4S], the catalytic site in nitrous oxide reductase, by EPR spectrocopy. Dalton Trans. (2004) 996-1002
15. Neese F., and Solomon E.I. MCD C-term signs, saturations behavior, and determination of band polarisations in randomly orientated systems with spin S >/ = (1)/(2) and S = (5)/(2). Inorg. Chem. 38 (1999) 1847-1865
16. 2O reductase. J. Am. Chem. Soc. 124 (2002) 744-745
17. Chan J.M., Bollinger J.A., Grewell C.L., and Dooley D.M. Reductively activated nitrous oxide reductase reacts directly with substrate. J. Am. Chem. Soc. 126 (2004) 3030-3031
18. Z, in the enzyme nitrous oxide reductase from Paracoccus pantotrophus. Biochem. J. 364 (2002) 807-815
19. Hulse C.L., and Averill B.A. Isolation of a high specific activity pink, monomeric nitrous oxide reductase from Acromobacter cycloclastes. Biochem. Biophys. Res. Commun. 166 (1990) 729-735
20. Jones S., and Thornton J.M. Principles of protein-protein interactions. Proc. Natl Acad. Sci. USA 93 (1996) 13-20
21. Murshudov G.N., and Dodson E.J. Simplified error estimation a la Cruickshank in macromolecular crystallography. In: Winn M. (Ed). CCP4 Newsletter on Protein Crystallography . 33 (1997), Daresbury Laboratory 31-39
22. Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum likelihood method. Acta Crystallog. sect. D 53 (1997) 240-255
23. Charnock J.M., Dreusch A., Korner H., Neese F., Nelson J., Kannt A., et al. Structural investigations of the Cu-A centre of nitrous oxide reductase from Pseudomonas stutzeri by site-directed mutagenesis and X-ray absorption spectroscopy. Eur. J. Biochem. 267 (2000) 1368-1381
24. Liu M.Y., Liu M.C., Payne W.J., and Legall J. Properties and electron transfer specificity of copper proteins from the denitrifier Achromobacter cycloclastes. J. Bacteriol. 166 (1986) 604-608
25. Libby E., and Averill B.A. Evidence that the type-2 copper centers are the site of nitrite reduction by Achromobacter cycloclastes nitrite reductase. Biochem. Biophys. Res. Comms. 187 (1992) 1529-1535
26. Ferretti S., Grossmann J.G., Hasnain S.S., Eady R.R., and Smith B.E. Biochemical characterization and solution structure of nitrous oxide reductase from Alcaligenes xylosoxidans (NCIMB 11015). Eur. J. Biochem. 259 (1999) 651-659
27. Cianci M., Antonyuk S., Bliss N., Buffey S.G., Cheung K.C., Clarke J.A., et al. A high-throughput structural biology/proteomics beamline at the SRS on a new multipole wiggler. J. Synchr. Rad. 12 (2005) 442-452
28. Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
29. Vagin A.A., and Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallog. 30 (1997) 1022-1025
30. Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallog. sect. D 60 (2004) 2126-2132
31. Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A 47 (1991) 110-119