Aminobacter aminovorans NADH:Flavin oxidoreductase His140: A highly conserved residue critical for NADH binding and utilization

Biochemistry

Volumn 43, Issue 40, 2004, Pages 12887-12893

  Russell, Thomas R ^a   Tu, Shiao Chun ^a  

^a University of Houston   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASSAYS; FILTRATION; FLUORESCENCE; MUTAGENESIS; PROTEINS; QUENCHING; REACTION KINETICS; STOICHIOMETRY;

ANAEROBIC REDUCTION; FLAVIN OXIREDUCTASE; FLAVOPROTEINS; KINETIC MECHANISMS;

ENZYMES;

FLAVOPROTEIN; HISTIDINE; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE;

AMINOBACTER AMINOVORANS; ARTICLE; BACTERIUM; CATALYSIS; ENZYME ACTIVE SITE; ENZYME BINDING; GENETIC CONSERVATION; KINETICS; NONHUMAN; PRIORITY JOURNAL; REDUCTION; SEQUENCE ALIGNMENT; STOICHIOMETRY; ULTRAFILTRATION;

ALPHAPROTEOBACTERIA; AMINO ACID SEQUENCE; ANAEROBIOSIS; FLAVINS; FMN REDUCTASE; HISTIDINE; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NAD; OXIDATION-REDUCTION; SEQUENCE ALIGNMENT; SPECTRUM ANALYSIS;

AMINOBACTER; AMINOBACTER AMINOVORANS; BACTERIA (MICROORGANISMS);

EID: 4944228606     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048499n     Document Type: Article

References (35)

1. Tu, S.-C. (2001) Reduced flavin: Donor and acceptor enzymes and mechanisms of channeling, Antioxid. Redox Signaling 3, 881-897.
2. Low, J. C., and Tu, S.-C. (2002) Functional roles of conserved residues in the unstructured loop of Vibrio harveyi bacterial luciferase, Biochemistry 41, 1724-1731.
3. Low, J. C., and Tu, S.-C. (2003) Energy transfer evidence for in vitro and in vivo complexes of Vibrio harveyi flavin reductase P and luciferase, Photochem. Photobiol. 77, 446-452.
4. Kendrew, S. G., Harding, S. E., Hopwood, D. A., and Marsh, E. N. (1995) Identification of a flavin:NADH oxidoreductase involved in the biosynthesis of actinorhodin. Purification and characterization of the recombinant enzyme, J. Biol. Chem. 270, 17339-17343.
5. Kendrew, S. G., Hopwood, D. A., and Marsh, E. N. (1997) Identification of a monooxygenase from Streptomyces coelicolor A3(2) involved in biosynthesis of actinorhodin: Purification and characterization of the recombinant enzyme, J. Bacteriol. 179, 4305-4310.
6. Xun, L. (1996) Purification and characterization of chlorophenol 4-monooxygenase from Burkholderia cepacia AC1100, J. Bacteriol. 178, 2645-2649.
7. Gisi, M. R., and Xun, L. (2003) Characterization of chlorophenol 4-monooxygenase (TftD) and NADH:flavin adenine dinucleotide oxidoreductase (TftC) of Burkholderia cepacia AC1100, J. Bacteriol. 185, 2786-2792.
8. Russell, T. R., Demeler, B., and Tu, S. C. (2004) Kinetic mechanism and quaternary structure of Aminobacter aminovorans NADH:flavin oxidoreductase: An unusual flavin reductase with bound flavin, Biochemistry 43, 1580-1590.
9. Gerlo, E., and Charlier, J. (1975) Identification of NADH-specific and NADPH-specific FMN reductases in Beneckea harveyi, Eur. J. Biochem. 57, 461-467.
10. Jablonski, E., and DeLuca, M. (1978) Studies of the control of luminescence in Beneckea harveyi: Properties of the NADH and NADPH:FMN oxidoreductases, Biochemistry 17, 672-678.
11. Lei, B., Liu, M., Huang, S., and Tu, S.-C. (1994) Vibrio harveyi NADPH-flavin oxidoreductase: Cloning, sequencing, and overexpression of the gene and purification and characterization of the cloned enzyme, J. Bacteriol. 176, 3552-3558.
12. Liu, M., Lei, B., Ding, Q., Lee, J. C., and Tu, S.-C. (1997) Vibrio harveyi NADPH:FMN oxidoreductase: Preparation and characterization of the apoenzyme and monomer-dimer equilibrium, Arch. Biochem. Biophys. 337, 89-95.
13. Tanner, J. J., Lei, B., Tu, S.-C., and Krause, K. L. (1996) Flavin reductase P: Structure of a dimeric enzyme that reduces flavin, Biochemistry 35, 13531-13539.
14. Inouye, S. (1994) NAD(P)H-flavin oxidoreductase from the bioluminescent bacterium, Vibrio fischeri ATCC 7744, is a flavoprotein, FEBS Lett. 347, 163-168.
15. Zenno, S., Saigo, K., Kanoh, H., and Inouye, S. (1994) Identification of the gene encoding the major NAD(P)H-flavin oxidoreductase of the bioluminescent bacterium Vibriofischeri ATCC 7744, J. Bacteriol. 176, 3536-3543.
16. Tang, C. K., Jeffers, C. E., Nichols, J. C., and Tu, S.-C. (2001) Flavin specificity and subunit interaction of Vibriofischeri general NAD(P)H-flavin oxidoreductase FRG/FRase I, Arch. Biochem. Biophys. 392, 110-116.
17. Koike, H., Sasaki, H., Kobori, T., Zenno, S., Saigo, K., Murphy, M. E., Adman, E. T., and Tanokura, M. (1998) 1.8 Å crystal structure of the major NAD(P)H:FMN oxidoreductase of a bioluminescent bacterium, Vibrio fischeri: Overall structure, cofactor and substrate-analog binding, and comparison with related flavoproteins, J. Mol. Biol. 280, 259-273.
18. Fieschi, F., Nivière, V., Frier, C., Décout, J.-L., and Fontecave, M. (1995) The mechanism and substrate specificity of the NADPH:flavin oxidoreductase from Escherichia coli, J. Biol. Chem. 270, 30392-30400.
19. Louie, T. M., Yang, H., Karnchanaphanurach, P., Xie, X. S., and Xun, L. (2002) FAD is a preferred substrate and an inhibitor of Escherichia coli general NAD(P)H:flavin oxidoreductase, J. Biol. Chem. 277, 39450-39455.
20. Filisetti, L., Fontecave, M., and Niviere, V. (2003) Mechanism and substrate specificity of the flavin reductase ActVB from Streptomyces coelicolor, J. Biol. Chem. 278, 296-303.
21. Bucheli-Witschel, M., and Egli, T. (2001) Environmental fate and microbial degradation of aminopolycarboxylic acids, FEMS Microbiol. Rev. 25, 69-106.
22. Jeffers, C. E., Nichols, J. C., and Tu, S.-C. (2003) Complex formation between Vibrio harveyi luciferase and monomeric NADPH:FMN oxidoreductase, Biochemistry 42, 529-534.
23. Galán, B., Díaz, E., Prieto, M. A., and García, J. L. (2000) Functional analysis of the small component of the 4- hydroxyphenylacetate 3-monooxygenase of Escherichia coli W: A prototype of a new flavin:NAD(P)H reductase subfamily, J. Bacteriol. 182, 627-636.
24. Wang, H., Lei, B., and Tu, S.-C. (2000) Vibrio harveyi NADPH-FMN oxidoreductase Arg203 as a critical residue for NADPH recognition and binding, Biochemistry 39, 7813-7819.
25. Ausubel, M. F. (1993) in Current Protocols in Molecular Biology, John Wiley and Sons: New York.
26. Tu, S.-C., and McCormick, D. B. (1974) Conformation of porcine D-amino acid oxidase as studied by protein fluorescence and optical rotatory dispersion, Biochemistry 13, 893-899.
27. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
28. Altschul, S. F., Gish, W., Miller, W., Myers, E. W., and Lipman, D. J. (1990) Basic Local Alignment Search Tool, J. Mol. Biol. 215, 403-410.
29. Marchler-Bauer, A., Panchenko, A. R., Shoemaker, B. A., Thiessen, P. A., Geer, L. Y., and Bryant, S. H. (2002) CDD: A database of conserved domain alignments with links to domain three-dimensional structure, Nucleic Acids Res. 30, 281-283.
30. Marchler-Bauer, A., Anderson, J. B., DeWeese-Scott, C., Fedorova, N. D., Geer, L. Y., He, S., Hurwitz, D. I., Jackson, J. D., Jacobs, A. R., Lanczycki, C. J., Liebert, C. A., Liu, C., Madej, T., Marchler, G. H., Mazumder, R., Nikolskaya, A. N., Panchenko, A. R., Rao, B. S., Shoemaker, B. A., Simonyan, V., Song, J. S., Thiessen, P. A., Vasudevan, S., Wang, Y., Yamashita, R. A., Yin, J. J., and Bryant, S. H. (2003) CDD: A curated Entrez database of conserved domain alignments, Nucleic Acids Res. 31, 383-387.
31. Thompson, J. D., Higgins, D. G., and Gibson, T. J. (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.
32. Smith, R. F., Wiese, B. A., Wojzynski, M. K., Davison, D. B., and Worley, K. C. (1996) BCM search launcher-An integrated interface to molecular biology database search and analysis services available on the World Wide Web, Genome Res. 6, 454-462.
33. Berman, H. M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T. N., Weissig, H., Shindyalov, I. N., and Bourne, P. E. (2000) The Protein Data Bank, Nucleic Acids Res. 28, 235-242.
34. +, Structure 9, 311-319.
35. Kirchner, U., Westphal, A. H., Muller, R., and van Berkel, W. J. (2003) Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual role for FAD, J. Biol. Chem. 278, 47545-47553.