Functional role of Trp-105 of Enterococcus faecalis azoreductase (AzoA) as resolved by structural and mutational analysis

References

1. Chen H. 2006; Recent advances in azo dye degrading enzyme research. Curr Protein Pept Sci 7:101–111
   [Google Scholar]
2. Chen H., Wang R. F., Cerniglia C. E. 2004; Molecular cloning, overexpression, purification, and characterization of an aerobic FMN-dependent azoreductase from Enterococcus faecalis . Protein Expr Purif 34:302–310
   [Google Scholar]
3. Chen H., Hopper S. L., Cerniglia C. E. 2005; Biochemical and molecular characterization of an azoreductase from Staphylococcus aureus , a tetrameric NADPH-dependent flavoprotein. Microbiology 151:1433–1441
   [Google Scholar]
4. Chung K. T. 1983; The significance of azo-reduction in the mutagenesis and carcinogenesis of azo dyes. Mutat Res 114:269–281
   [Google Scholar]
5. Deller S., Sollner S., Trenker-El-Toukhy R., Jelesarov I., Gubitz G. M., Macheroux P. 2006; Characterization of a thermostable NADPH : FMN oxidoreductase from the mesophilic bacterium Bacillus subtilis . Biochemistry 45:7083–7091
   [Google Scholar]
6. Eckburg P. B., Bik E. M., Bernstein C. N., Purdom E., Dethlefsen L., Sargent M., Gill S. R., Nelson K. E., Relman D. A. 2005; Diversity of the human intestinal microbial flora. Science 308:1635–1638
   [Google Scholar]
7. Hanauer S. B. 1996; Inflammatory bowel disease. N Engl J Med 334:841–848
   [Google Scholar]
8. Ito K., Nakanishi M., Lee W. C., Sasaki H., Zenno S., Saigo K., Kitade Y., Tanokura M. 2006; Three-dimensional structure of AzoR from Escherichia coli . An oxidoreductase conserved in microorganisms. J Biol Chem 281:20567–20576
   [Google Scholar]
9. Laemmli U. K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685
   [Google Scholar]
10. Li Z., Meighen E. A. 1995; Tryptophan 250 on the alpha subunit plays an important role in flavin and aldehyde binding to bacterial luciferase. Effects of W→Y mutations on catalytic function. Biochemistry 34:15084–15090
    [Google Scholar]
11. Liu Z. J., Chen H., Shaw N., Hopper S. L., Chen L., Chen S., Cerniglia C. E., Wang B. C. 2007; Crystal structure of an aerobic FMN-dependent azoreductase (AzoA) from Enterococcus faecalis . Arch Biochem Biophys 463:68–77
    [Google Scholar]
12. Lostao A., Gomez-Moreno C., Mayhew S. G., Sancho J. 1997; Differential stabilization of the three FMN redox forms by tyrosine 94 and tryptophan 57 in flavodoxin from Anabaena and its influence on the redox potentials. Biochemistry 36:14334–14344
    [Google Scholar]
13. Lostao A., Daoudi F., Irun M. P., Ramon A., Fernandez-Cabrera C., Romero A., Sancho J. 2003; How FMN binds to Anabaena apoflavodoxin: a hydrophobic encounter at an open binding site. J Biol Chem 278:24053–24061
    [Google Scholar]
14. Maiti R., Van Domselaar G. H., Zhang H., Wishart D. S. 2004; SuperPose: a simple server for sophisticated structural superposition. Nucleic Acids Res 32:W590–W594
    [Google Scholar]
15. McDonald I. K., Thornton J. M. 1994; Satisfying hydrogen bonding potential in proteins. J Mol Biol 238:777–793
    [Google Scholar]
16. Milburn D., Laskowski R. A., Thornton J. M. 1998; Sequences annotated by structure: a tool to facilitate the use of structural information in sequence analysis. Protein Eng 11:855–859
    [Google Scholar]
17. Murray T. A., Swenson R. P. 2003; Mechanism of flavin mononucleotide cofactor binding to the Desulfovibrio vulgaris flavodoxin. 1. Kinetic evidence for cooperative effects associated with the binding of inorganic phosphate and the 5′-phosphate moiety of the cofactor. Biochemistry 42:2307–2316
    [Google Scholar]
18. Platzek T., Lang C., Grohmann G., Gi U. S., Baltes W. 1999; Formation of a carcinogenic aromatic amine from an azo dye by human skin bacteria in vitro . Hum Exp Toxicol 18:552–559
    [Google Scholar]
19. Schwede T., Kopp J., Guex N., Peitsch M. C. 2003; SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res 31:3381–3385
    [Google Scholar]
20. Sobolev V., Sorokine A., Prilusky J., Abola E. E., Edelman M. 1999; Automated analysis of interatomic contacts in proteins. Bioinformatics 15:327–332
    [Google Scholar]
21. Stolz A. 2001; Basic and applied aspects in the microbial degradation of azo dyes. Appl Microbiol Biotechnol 56:69–80
    [Google Scholar]
22. Velec H. F., Gohlke H., Klebe G. 2005; DrugScore (CSD)-knowledge-based scoring function derived from small molecule crystal data with superior recognition rate of near-native ligand poses and better affinity prediction. J Med Chem 48:6296–6303
    [Google Scholar]
23. Wallace A. C., Laskowski R. A., Thornton J. M. 1995; LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng 8:127–134
    [Google Scholar]
24. Wang C. J., Hagemeier C., Rahman N., Lowe E., Noble M., Coughtrie M., Sim E., Westwood I. 2007; Molecular cloning, characterisation and ligand-bound structure of an azoreductase from Pseudomonas aeruginosa . J Mol Biol 373:1213–1228
    [Google Scholar]
25. Wu K., Knox R., Sun X. Z., Joseph P., Jaiswal A. K., Zhang D., Deng P. S., Chen S. 1997; Catalytic properties of NAD(P)H : quinone oxidoreductase-2 (NQO2), a dihydronicotinamide riboside dependent oxidoreductase. Arch Biochem Biophys 347:221–228
    [Google Scholar]