Reduction kinetics of a flavin oxidoreductase LuxG from photobacterium leiognathi (TH1): Half-sites reactivity

Biochemistry

Volumn 49, Issue 43, 2010, Pages 9241-9248

  Nijvipakul, Sarayut ^a   Ballou, David P ^b   Chaiyen, Pimchai ^a  

^a Mahidol University ^*  (Thailand)

^b UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ABSORBANCES; BI-PHASIC; BURST KINETICS; FLAVIN REDUCTASE; FUNCTIONAL FORMS; KINETIC DATA; KINETIC ISOTOPE EFFECTS; LABELED SUBSTRATES; MONOOXYGENASES; OVERALL REACTIONS; OXIDOREDUCTASES; PHOTOBACTERIUM LEIOGNATHI; PYRIDINE NUCLEOTIDES; REACTIVITY MODELS; REDUCTION KINETICS; REDUCTION PHASE; SECOND PHASE; STEADY-STATE KINETICS; STOPPED-FLOW SPECTROPHOTOMETRY; TRANSIENT KINETICS; TURNOVER NUMBER; TWO-COMPONENT;

ALDEHYDES; BACTERIOLOGY; CHARGE TRANSFER; COENZYMES; ISOTOPES; NUCLEOTIDES; PLANTS (BOTANY); RATE CONSTANTS; REACTION INTERMEDIATES; SPECTROPHOTOMETRY;

REACTION KINETICS;

ALKANAL MONOOXYGENASE (FMN LINKED); FLAVINE MONONUCLEOTIDE; ISOTOPE; OXIDOREDUCTASE; PYRIDINE NUCLEOTIDE; QUERCETIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

ARTICLE; BIOLUMINESCENCE; ENZYME BINDING; ENZYME KINETICS; KINETICS; NONHUMAN; OPERON; OXIDATION; PHOTOBACTERIUM LEIOGNATHI; PRIORITY JOURNAL; REDUCTION KINETICS; SPECTROPHOTOMETRY; STEADY STATE;

BACTERIAL PROTEINS; CATALYSIS; FLAVIN MONONUCLEOTIDE; FLAVINS; KINETICS; LUCIFERASES; LUMINESCENT PROTEINS; NAD; OXIDOREDUCTASES; PHOTOBACTERIUM; SPECTRUM ANALYSIS;

BACTERIA (MICROORGANISMS); PHOTOBACTERIUM LEIOGNATHI;

EID: 78049255927     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1009985     Document Type: Article

References (39)

1. Fontecave, M., Coves, J., and Pierre, J. L. (1994) Ferric reductases or flavin reductases? Biometals. 7, 3-8
2. Hasan, N. and Nester, E. W. (1978) Purification and characterization of NADPH-dependent flavin reductase. An enzyme required for the activation of chorismate synthase in Bacillus subtilis J. Biol. Chem. 253, 4987-4992
3. Fontecave, M., Eliasson, R., and Reichard, P. (1987) NAD(P)H:flavin oxidoreductase of Escherichia coli. A ferric iron reductase participating in the generation of the free radical of ribonucleotide reductase J. Biol. Chem. 262, 12325-12331
4. Ballou, D. P., Entsch, B., and Cole, L. J. (2005) Dynamics involved in catalysis by single-component and two-component flavin-dependent aromatic hydroxylases Biochem. Biophys. Res. Commun. 338, 590-598
5. Van Berkel, W. J., Kamerbeek, N. M., and Fraaije, M. W. (2006) Flavoprotein monooxygenases, a diverse class of oxidative biocatalysis J. Biotechnol. 124, 760-789
6. Ellis, H. R. (2010) The FMN-dependent two-component monooxygenase systems Arch. Biochem. Biophys. 497, 1-12
7. Chaiyen, P., Suadee, C., and Wilairat, P. (2001) A novel two-protein component flavoprotein hydroxylase Eur. J. Biochem. 268, 5550-5561
8. Arunachalam, U., Massey, V., and Miller, S. M. (1994) Mechanism of p -hydroxyphenylacetate-3-hydroxylase. A two-protein enzyme J. Biol. Chem. 269, 150-155
9. Valton, J., Filisetti, L., Fontecave, M., and Niviere, V. (2004) A two-component flavin-dependent monooxygenase involved in actinorhodin biosynthesis in Streptomyces coelicolor J. Biol. Chem. 279, 44362-44369
10. Nijvipakul, S., Wongratana, J., Suadee, C., Entsch, B., Ballou, D. P., and Chaiyen, P. (2008) LuxG is a functioning flavin reductase for bacterial luminescence J. Bacteriol. 190, 1531-1538
11. Suadee, C., Nijvipakul, S., Svasti, J., Entsch, B., Ballou, D. P., and Chaiyen, P. (2007) Luciferase from Vibrio campbellii is more thermostable and binds reduced FMN better than its homologues J. Biochem. 142, 539-552
12. Campbell, Z. T. and Baldwin, T. O. (2009) Fre is the major flavin reductase supporting bioluminescence from Vibrio harveyi luciferase in Escherichia coli J. Biol. Chem. 284, 8322-8328
13. 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 Vibrio fischeri ATCC 7744 J. Bacteriol. 176, 3536-3543
14. 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
15. Tu, S. C. (2001) Reduced flavin: donor and acceptor enzymes and mechanisms of channeling Antioxid. Redox Signal. 3, 881-897
16. 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
17. Ingelman, M., Ramaswamy, S., Niviere, V., Fontecave, M., and Eklund, H. (1999) Crystal structure of NAD(P)H:flavin oxidoreductase from Escherichia coli Biochemistry. 38, 7040-7049
18. Fieschi, F., Niviere, V., Frier, C., Decout, 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. Niviere, V., Fieschi, F., Decout, J. L., and Fontecave, M. (1999) The NAD(P)H:flavin oxidoreductase from Escherichia coli. Evidence for a new mode of binding for reduced pyridine nucleotides J. Biol. Chem. 274, 18252-18260
20. Zenno, S. and Saigo, K. (1994) Identification of the genes encoding NAD(P)H-flavin oxidoreductases that are similar in sequence to Escherichia coli Fre in four species of luminous bacteria: Photorhabdus luminescens, Vibrio fischeri, Vibrio harveyi, and Vibrio orientalis J. Bacteriol. 176, 3544-3551
21. Sucharitakul, J., Chaiyen, P., Entsch, B., and Ballou, D. P. (2005) The reductase of p -hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii requires p -hydroxyphenylacetate for effective catalysis Biochemistry 44, 10434-10442
22. Gassner, G., Wang, L., Batie, C., and Ballou, D. P. (1994) Reaction of phthalate dioxygenase reductase with NADH and NAD: kinetic and spectral characterization of intermediates Biochemistry 33, 12184-12193
23. Patil, P. V. and Ballou, D. P. (2000) The use of photocatechuate dioxygenase for maintaining anaerobic conditions in biochemical experiments Anal. Biochem. 286, 187-192
24. Hiromi, K. (1979) Analysis of Fast Enzyme Reactions: Transient Kinetics, Kinetics of Fast Enzyme Reactions: Theory and Practice, pp 187 - 244, Kodansha Ltd., Tokyo.
25. Gassner, G. T. and Ballou, D. P. (1995) Preparation and characterization of a truncated form of phthalate dioxygenase reductase that lacks an iron-sulfur domain Biochemistry 34, 13460-13471
26. Niviere, V., Vanoni, M. A., Zanetti, G., and Fontecave, M. (1998) Reaction of the NAD(P)H:flavin oxidoreductase from Escherichia coli with NADPH and riboflavin: identification of intermediates Biochemistry 37, 11879-11887
27. Karplus, P. A. and Bruns, C. M. (1994) Structure-function relations for ferredoxin reductase J. Bioenerg. Biomembr. 26, 89-99
28. + reductase. Rapid-reaction evidence for participation of a ternary complex J. Biol. Chem. 259, 11976-11985
29. + reductase with NADP(H) specificity and oxidation-reduction properties J. Biol. Chem. 261, 11214-11223
30. Seydoux, F., Malhotra, O. P., and Bernhard, S. A. (1974) Half-site reactivity CRC Crit. Rev. Biochem. 2, 227-257
31. Inouye, S. (1994) NAD(P)H-flavin oxidoreductase from the bioluminescent bacterium, Vibrio fischeri ATCC 7744, is a flavoprotein FEBS Lett. 347, 163-168
32. Lei, B. and Tu, S. C. (1998) Mechanism of reduced flavin transfer from Vibrio harveyi NADPH-FMN oxidoreductase to luciferase Biochemistry 37, 14623-14629
33. Meighen, E. A. (1994) Genetics of bacterial bioluminescence Annu. Rev. Genet. 28, 117-139
34. Thotsaporn, K., Sucharitakul, J., Wongratana, J., Suadee, C., and Chaiyen, P. (2004) Cloning and expression of p- hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii: evidence of the divergence of enzymes in the class of two-protein component aromatic hydroxylases Biochim. Biophys. Acta 1680, 60-66
35. Sucharitakul, J., Chaiyen, P., Entsch, B., and Ballou, D. P. (2006) Kinetic mechanisms of the oxygenase from a two-component enzyme, p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii J. Biol. Chem. 281, 17044-17053
36. Sucharitakul, J., Phongsak, T., Entsch, B., Svasti, J., Chaiyen, P., and Ballou, D. P. (2007) Kinetics of a two-component p -hydroxyphenylacetate hydroxylase explain how reduced flavin is transferred from the reductase to the oxygenase Biochemistry 46, 8611-8623
37. 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
38. Valton, J., Mathevon, C., Fontecave, M., Niviere, V., and Ballou, D. P. (2008) The two-component FMN-dependent monooxygenase ActVA-ActVB from Streptomyces coelicolor: mechanism and regulation J. Biol. Chem. 283, 10287-10296
39. Gao, B. and Ellis, H. R. (2007) Mechanism of flavin reduction in the alkanesulfonate monooxygenase system Biochim. Biophys. Acta 1774, 359-367