The reductase of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii requires p-hydroxyphenylacetate for effective catalysis

Biochemistry

Volumn 44, Issue 30, 2005, Pages 10434-10442

  Sucharitakul, Jeerus ^a   Chaiyen, Pimchai ^a   Entsch, Barrie ^b   Ballou, David P ^b  

^a MAHIDOL UNIVERSITY   (Thailand)

^b UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; BIODIVERSITY; CATALYSIS; ENZYMES; HYDROXYLATION; OXIDATION; REDOX REACTIONS; THERMODYNAMICS;

LARGER OXYGENASE COMPONENT; NADH BINDING; REDOX POTENTIAL; SMALLER REDUCTASE COMPONENT;

PROTEINS;

3,4 DIHYDROXYPHENYLACETIC ACID; 4 HYDROXYPHENYLACETATE 3 HYDROXYLASE; 4 HYDROXYPHENYLACETIC ACID; ENZYME; FLAVOPROTEIN; OXIDOREDUCTASE; OXYGENASE; QUERCETIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; UNCLASSIFIED DRUG;

ACINETOBACTER BAUMANNII; ARTICLE; CATALYSIS; CHEMICAL REACTION; HYDROXYLATION; NONHUMAN; OXIDATION REDUCTION POTENTIAL; PRIORITY JOURNAL; REACTION ANALYSIS; THERMODYNAMICS;

ACINETOBACTER BAUMANNII; APOENZYMES; CATALYSIS; FLAVIN MONONUCLEOTIDE; HYDROXYLATION; KINETICS; MIXED FUNCTION OXYGENASES; MODELS, CHEMICAL; NAD; OXIDATION-REDUCTION; OXIDOREDUCTASES; OXYGEN; PHENYLACETATES; PROTEIN BINDING; THERMODYNAMICS;

ACINETOBACTER BAUMANNII;

EID: 23044506644     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050615e     Document Type: Article

References (49)

1. Dagley, S. (1987) Lessons from biodegradation, Annu. Rev. Microbiol. 41, 1-23.
2. Arunachalam, U., Massey, V., and Vaidyanathan, C. S. (1992) p-Hydroxyphenylacetate-3-hydroxylase: A two-protein component enzyme, J. Biol. Chem. 267, 25848-25855.
3. Galan, B., Diaz, E., Prieto, M. A., and Garcia, J. L. (2000) Functional analysis of the small component of the 4-hydroxyphenylacetate 3-hydroxylase of Escherichia coli W: A prototype of a new flavin:NAD(P)H reductase subfamily, J. Bacteriol. 182, 627-636.
4. Chaiyen, P., Suadee, C., and Wilairat, P. (2001) A novel two-protein component flavoprotein hydroxylase: p-Hydroxyphenylacetate hydroxylase from Acinetobacter baumannii, Eur. J. Biochem. 268, 5550-5561.
5. 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.
6. Palfey, B. A., and Massey, V. (1998) Flavin-dependent enzymes, in Comprehensive Biological Catalysis (Michael, S., Ed.) Vol. 3, pp 83-153, Academic Press, San Diego.
7. Palfey, B. A., Ballou, D. P., and Massey, V. (1995) Oxygen activation by flavins and pterins, in Active Oxygen in Biochemistry (Valentine, J. S., Foote, C. S., Greenberg, A., and Liebman, J. F., Eds.) pp 37-83, Chapman & Hall, Glasgow, Scotland.
8. Xun, L., and Sandvik, E. R. (2000) Characterization of 4-hydroxyphenylacetate 3-hydroxylase (HpaB) of Escherichia coli as a reduced flavin adenine dinucleotide-utilizing monooxygenase, Appl. Environ. Microbiol. 66, 481-486.
9. 2 by NAD(P)H-flavin oxidoreductase and 4-hydroxyphenylacetate 3-monooxygenase, Biochemistry 42, 7509-7517.
10. 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.
11. Kim, I. C., and Oriel, P. J. (1995) Characterization of the Bacillus stearothermophilus BR219 phenol hydroxylase gene, Appl. Environ. Microbiol. 61, 1252-1256.
12. Kirchner, U., Westphal, A. H., Muller, R., and van Berkel, W. J. H. (2003) Phenol hydroxylase from Bacillus thermoglucosidasius A7: A two-protein component monooxygenase with dual role for FAD, J. Biol. Chem. 278, 47545-47553.
13. 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.
14. Louie, T. M., Webste, C. M., and Xun, L. (2002) Genetic and biochemical characterization of a 2,4,6-trichlorophenol degradation pathway in Ralstonia eurropha JMP134, J. Bacteriol. 184, 3492-3500.
15. Becker, D., Schrader, T., and Andreesen, J. R. (1997) Two-component flavin-dependent pyrrole-2-carboxylate monooxygenase from Rhodococcus sp., Eur. J. Biochem. 249, 739-747.
16. Otto, K., Hofstetter, K., Rothlisberger, M., Witholt, B., and Schmid, A. (2004) Biochemical characterization of StyAB from Pseudomonas sp. strain VLB120 as a two-component flavin-diffusible monooxygenase, J. Bacteriol. 186, 5292-5302.
17. Kadiyala, V., and Spain, J. C. (1998) A two-component monooxygenase catalyzes both the hydroxylation of p-nitrophenol and the oxidative release of nitrite from 4-nitrocatechol in Bacillus sphaericus JS905, Appl. Environ. Microbiol. 64, 2479-2484.
18. Uetz, T., Schneider, R., Snozzi, M., and Egli, A. (1992) Purification and characterization of two-component monooxygenase that hydroxylates nitrilotriacetate from Chelatobacter strain ATCC 29600, J. Bacteriol. 174, 1179-1188.
19. Xu, Y., Mortimer, M. W., Fisher, T. S., Kahn, M. L., Brockman, F. J., and Xun, L. (1997) Cloning, sequencing and analysis of a gene cluster from Chelatobacter heiztzii ATCC 29600 encoding nitrilotriacetate monooxygenase and NADH:flavin mononucleotide oxidoreductase, J. Bacteriol. 79, 1112-1116.
20. Witschel, M., Nigel, S., and Egli, T. (1997) Identification and characterization of the two-enzyme system catalyzing oxidation of EDTA in the EDTA-degrading bacterial strain DSM 9103, J. Bacteriol. 179, 6937-6943.
21. Eichhorn, E., van der Ploeg, J. R., and Leisinger, T. (1999) Characterization of a two-component alkanesulfonate monooxygenase from Escherichia coli, J. Biol. Chem. 274, 26639-26646.
22. Hastings, J. W. (1996) Chemistries and colors of bioluminescent reactions: A review, Gene 173, 5-11.
23. Lei, B., and Tu, S.-C. (1998) Mechanism of reduced flavin transfer from Vibrio harveyi NADPH-FMN oxidoreductase to luciferase. Biochemistry 37, 14623-14629.
24. 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.
25. 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.
26. Thibaut, D., Ratet, N., Bisch, D., Faucher, D., Debussche, L., and Blanche, F. (1995) Purification of the two-enzyme system catalyzing the oxidation of the D-proline residue of pristinamycin IIB during the last step of pristinamycin IIA biosynthesis, J. Bacteriol. 177, 5199-5205.
27. Parry, R. J., and Li, W. (1997) Purification and characterization of isobutylamine N-hydroxylase from the valanimycin producer Streptomyces viridifaciens MG456-hF10, Arch. Biochem. Biophys. 339, 47-54.
28. Duch, D. S., and Laskowski, M., Sr. (1971) A sensitive method for the determination of RNA in DNA and vice versa, Anal. Biochem. 44, 42-48.
29. 2H] NAD(P)H and determination of the stereospecificity of 7-α- and 12-α-hydroxysteroid dehydrogenase, Biochim. Biophys. Acta 998, 173-178.
30. Newton, C. J., Faynor, S. M., and Northrup, D. B. (1983) Purification of reduced nicotinamide dinucleotide by ion-exchange and high-performance liquid chromatography, Anal. Biochem. 132, 50-53.
31. Williams, C. H. J. R., Arscott, L. D., Matthews, R. G., Thorpe, C., and Wilkinson, K. D. (1979) Methodology employed for anaerobic spectrophotometric titrations and for computer-assisted data analysis, Methods Enzymol. 62, 185-198.
32. Massey, V. (1991) A Simple Method for the Determination of Redox Potentials, in Flavins and Flavoproteins (Curti, B., Rochi, S., and Zanetti, G., Eds.) pp 59-66, Water DeGruyter & Co., Berlin.
33. Loach, P. A. (1973) Oxidation-reduction potentials: Absorbance bands and molar absorbance of compounds used in biochemical studies, in Handbook of Biochemistry Selected Data for Molecular Biology (Sorber, H. A., Ed.) pp J-33-J-40, The Chemical Rubber Co. (CRC Press), Cleveland, OH.
34. Hiromi, K. (1979) Analysis of fast enzyme reactions: Transient kinetics, in Kinetics of Fast Enzyme Reactions, pp 193-194, Kodansha, Ltd. (Halsted Press), Tokyo.
35. Strickland, S., Palmer, G., and Massey, V. (1975) Determination of dissociation constants and specific rate constants of enzyme-substrate (or protein-ligand) interactions from rapid reaction kinetic data, J. Biol. Chem. 250, 4048-4052.
36. Massey, V., Palmer, G., and Ballou, D. P. (1971) On the reaction of reduced flavins and flavoproteins with molecular oxygen, in Flavins and Flavoproteins (Kamin, H., Ed.) pp 349-361, University Park Press, Baltimore.
37. Entsch, B., Cole, L. J., and Ballou, D. P. (2005) Protein dynamics and electrostatics In the function of p-hydroxybenzoate hydroxylase, Arch. Biochem. Biophys. 433, 297-311.
38. Powlowski, J., Ballou, D. P., and Massey, V. (1989) A rapid reaction study of anthranilate hydroxylase, J. Biol. Chem. 264, 16008-16016.
39. Chaiyen, P., Brissette, P., Ballou, D. P., and Massey, V. (1997) Thermodynamics reduction kinetics properties of 2-methyl-3-hydroxypyridine-5- carboxylic acid oxygenase, Biochemistry 36, 2612-2621.
40. Chaiyen, P., Brissette, P., Ballou, D. P., and Massey, V. (1997) Reaction of 2-methyl-3-hydroxypyridine-5-carboxylic acid (MHPC) oxygenase with N-methyl-5-hydroxynicotinic acid: Studies on the mode of binding, and protonation status of the substrate, Biochemistry 36, 13856-13864.
41. Chaiyen, P., Sucharitakul, J., Svasti, J., Entsch, B., Massey, V., and Ballou, D. P. (2004) Use of 8-substituted-FAD analogues to investigate the hydroxylation of the flavoprotein 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase, Biochemistry 43, 3933-3943.
42. Suske, W. A., van Berkel, W. J. H., and Kohler, H. P. E. (1999) Catalytic mechanism of 2-hydroxybiphenyl 3-monooxygenase, a flavoprotein from Pseudomonas azelaica HBP1, J. Biol. Chem. 274, 33355-33365.
43. Koder, R. L., Haynes, C. A., Rogers, M. E., Rogers, D. W., and Miller, A.-F. (2002) Flavin thermodynamics explain the oxygen insensitivity of enteric nitroreductases, Biochemistry 41, 14197-14205.
44. Kim, J.-J., Wang, M., and Paschke, R. (1993) Crystal structures of medium chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate, Proc. Natl. Acad. Sci. U.S.A. 90, 7523-7527.
45. Wang, R., and Thorpe, C. (1991) Reactivity of medium chain acyl-CoA dehydrogenase toward molecular oxygen, Biochemistry 30, 7895-7901.
46. Tu, S.-C. (2001) Reduced flavin: Donor and acceptor enzymes and mechanisms of channeling, Antioxid. Redox Signaling 3, 881-897.
47. Russell, T. R., and Tu, S.-C. (2004) Aminobacter aminovorans NADH:flavin oxidoreductase His140: A highly conserved residue critical for NADH binding and utilization, Biochemistry 43, 2887-2893.
48. Ballou, D. P. (1982) Flavoprotein Monooxygenases, in Flavins and Flavoproteins (Massey, V., and Williams, C. H., Eds.) pp 301-310, Elsevier North-Holland, New York.
49. Massey, V. (2000). The chemical and biological versatility of riboflavin, Biochem. Soc. Trans. 28, 283-296.