Structural and biochemical characterization of a quinol binding site of Escherichia coli nitrate reductase A

Journal of Biological Chemistry

Volumn 280, Issue 15, 2005, Pages 14836-14843

  Bertero, Michela G ^a   Rothery, Richard A ^b   Boroumand, Nasim ^b   Palak, Monica ^b   Blasco, Francis ^c   Ginet, Nicolas ^d   Weiner, Joel H ^b   Strynadka, Natalie C J ^a  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

^b UNIVERSITY OF ALBERTA   (Canada)

^c CNRS   (France)

^d UMR6191   (France)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CELL MEMBRANES; CRYSTAL STRUCTURE; ENZYME INHIBITION; ESCHERICHIA COLI; MUTAGENESIS; OXIDATION; PARAMAGNETIC RESONANCE; PHENOLS; PROTONS; SPECTRUM ANALYSIS;

NITRATE REDUCTASE; PENTACHLOROPHANOL; PROTON CONDUCTION; QUINOL BINDING SITE;

ENZYMES;

HEME; NITRATE REDUCTASE; PENTACHLOROPHENOL; QUINOLINIC ACID;

ARTICLE; ATOM; BACTERIAL MEMBRANE; BINDING SITE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ELECTRON SPIN RESONANCE; ELECTRON TRANSPORT; ENZYME ACTIVITY; ESCHERICHIA COLI; MOLECULAR MODEL; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN LOCALIZATION; PROTON TRANSPORT; SITE DIRECTED MUTAGENESIS;

BINDING SITES; CELL MEMBRANE; CRYSTALLOGRAPHY, X-RAY; DOSE-RESPONSE RELATIONSHIP, DRUG; ELECTRON SPIN RESONANCE SPECTROSCOPY; ESCHERICHIA COLI; HEME; HISTIDINE; HYDROXYQUINOLINES; KINETICS; LYSINE; MODELS, CHEMICAL; MODELS, MOLECULAR; MUTATION; NAPHTHOLS; NITRATE REDUCTASE; NITRATE REDUCTASES; OXIDOREDUCTASES; OXYGEN; PENTACHLOROPHENOL; PLASMIDS; PROTEIN BINDING; PROTONS; TERPENES; UBIQUINONE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 17644373498     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M410457200     Document Type: Article

References (38)

1. Bertero, M. G., Rather, R. A., Palak, M., Hou, C., Lim, D., Blasco, F., Weiner, J. H., and Strynadka, N. C. (2003) Nat. Struct. Biol. 10, 681-687
2. Blasco, F., Guigliarelli, B., Magalon, A., Asso, M., Giordano, G., and Rather, R. A. (2001) Cell. Mol. Life Sci. 58, 179-193
3. Mitchell, P. (1976) J. Theor. Biol. 62, 327-367
4. Jormakka, M., Tornroth, S., Byrne, B., and Iwata, S. (2002) Science 295, 1863-1868
5. Rather, R. A., Blasco, F., and Weiner, J. H. (2001) Biochemistry 40, 5260-5268
6. Rather, R. A., Blasco, F., Magalon, A., Asso, M., and Weiner, J. H. (1999) Biochemistry 38, 12747-12757
7. Magalon, A., Rather, R. A., Lemesle-Meunier, D., Frixon, C., Weiner, J. H., and Blasco, F. (1998) J. Biol. Chem. 273, 10851-10856
8. Zhao, Z., Rather, R. A., and Weiner, J. H. (2003) Biochemistry 42, 5403-5413
9. Zhao, Z., Rather, R. A., and Weiner, J. H. (2003) Biochemistry 42, 14225-14233
10. Pascal, M. C., Burini, J. F., Ratouchniak, J., and Chippaux, M. (1982) Mol. Gen. Genet 188, 103-106
11. Guigliarelli, B., Magalon, A., Asso, M., Bertrand, P., Frixon, C., Giordano, G., and Blasco, F. (1996) Biochemistry 35, 4828-4836
12. Rather, R. A., and Weiner, J. H. (1991) Biochemistry 30, 8296-8305
13. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951) J. Biol. Chem. 193, 265-275
14. Markwell, M. A., Haas, S. M., Bieber, L. L., and Tolbert, N. E. (1978) Anal. Biochem. 87, 206-210
15. Rather, R. A., Chatterjee, I., Kiema, G., McDermott, M. T., and Weiner, J. H. (1998) Biochem. J. 332, 35-41
16. Engel, P. C. (1996) Enzymology Labfax, pp. 100-109, Bios Scientific Publishing, San Diego, CA
17. Rather, R. A., and Weiner, J. H. (1998) Eur. J. Biochem. 254, 588-595
18. Okun, J. G., Lummen, P., and Brandt, U. (1999) J. Biol. Chem. 274, 2625-2630
19. Rather, R. A., Magalon, A., Giordano, G., Guigliarelli, B., Blasco, F., and Weiner, J. H. (1998) J. Biol. Chem. 273, 7462-7469
20. Rather, R. A., Grant, J. L., Johnson, J. L., Rajagopalan, K. V., and Weiner, J. H. (1995) J. Bacteriol. 177, 2057-2063
21. Johnson, J. L., Indermaur, L. W., and Rajagopalan, K. V. (1991) J. Biol. Chem. 266, 12140-12145
22. Otwinowski, Z. M., and Wladek, M. (1997) Methods Enzymol. 276, 307-326
23. Brunger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T., and Warren, G. L. (1998) Acta Crystallogr. D Biol. Crystallogr. 54, 905-921
24. McRee, D. E. (1999) J. Struct. Biol. 125, 156-165
25. Kraulis, P. J. (1991) J. Appl. Crystallogr. 24, 946-950
26. Bacon, D., and Anderson, W. (1988) J. Mol. Graph 24, 219-220
27. Wallace, B. J., and Young, I. G. (1977) Biochim. Biophys. Acta 461, 84-100
28. Brondijk, T. H., Fiegen, D., Richardson, D. J., and Cole, J. A. (2002) Mol. Microbiol. 44, 245-255
29. Maklashina, E., and Cecchini, G. (1999) Arch. Biochem. Biophys. 369, 223-232
30. Krissinel, E., and Henrick, K. (2004) Acta Crystallogr. Sect. D. Biol. Crystallogr. 60, 2256-2268
31. Rather, R. A., Blasco, F., Magalon, A., and Weiner, J. H. (2001) J. Mol. Microbiol. Biotechnol. 3, 273-283
32. Page, C. C., Moser, C. C., Chen, X., and Dutton, P. L. (1999) Nature 402, 47-52
33. Iverson, T. M., Luna-Chavez, C., Croal, L. R., Cecchini, G., and Rees, D. C. (2002) J. Biol. Chem. 277, 16124-16130
34. Fisher, N., and Rich, P. R. (2000) J. Mol. Biol. 296, 1153-1162
35. Iverson, T. M., Luna-Chavez, C., Cecchini, G., and Rees, D. C. (1999) Science 284, 1961-1966
36. Lancaster, C. R., Gorss, R., Haas, A., Ritter, M., Mantele, W., Simon, J., and Kroger, A. (2000) Proc. Natl. Acad. Sci. U. S. A. 97, 13051-13056
37. Hunte, C., Koepke, J., Lange, C., Rossmanith, T., and Michel, H. (2000) Structure Fold. Des. 8, 669-684
38. Honig, B., and Nicholls, A. (1995) Science 268, 1144-1149