Hydroquinone dioxygenase from Pseudomonas fluorescens ACB: A novel member of the family of nonheme-iron(II)-dependent dioxygenases

Journal of Bacteriology

Volumn 190, Issue 15, 2008, Pages 5199-5209

  Moonen, Mariëlle J H ^a   Synowsky, Silvia A ^b   Van Den Berg, Willy A M ^a   Westphal, Adrie H ^a   Heck, Albert J R ^b   Van Den Heuvel, Robert H H ^b,d   Fraaije, Marco W ^c   Van Berkel, Willem J H ^a  

^a WAGENINGEN UNIVERSITY   (Netherlands)

^b UTRECHT UNIVERSITY   (Netherlands)

^c UNIVERSITY OF GRONINGEN   (Netherlands)

^d NV ORGANON   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

1,10 PHENANTHROLINE; 2,2' BIPYRIDINE; 4 HYDROXYACETOPHENONE; 4 HYDROXYBENZOIC ACID; 4 HYDROXYMUCONIC SEMIALDEHYDE; ALDEHYDE DERIVATIVE; DIOXYGENASE; HYDROGEN PEROXIDE; HYDROQUINONE; HYDROQUINONE 1,2 DIOXYGENASE; IRON; PHENOL DERIVATIVE; TETRAMER;

ALPHA CHAIN; AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIAL GENE; BACTERIAL STRAIN; BETA CHAIN; CATABOLISM; CATALYSIS; ENZYME ACTIVATION; ENZYME PURIFICATION; GEL PERMEATION CHROMATOGRAPHY; GENE CLUSTER; GENE INACTIVATION; HAPC GENE; HAPD GENE; LIGAND BINDING; MASS SPECTROMETRY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NONHUMAN; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; PEPTIDE MAPPING; PRIORITY JOURNAL; PSEUDOMONAS FLUORESCENS; SEQUENCE ANALYSIS;

2,2'-DIPYRIDYL; ACETOPHENONES; AMINO ACID SEQUENCE; CHROMATOGRAPHY, GEL; DNA, BACTERIAL; ENZYME ACTIVATORS; ENZYME INHIBITORS; ENZYME STABILITY; FATTY ACIDS, UNSATURATED; HYDROGEN PEROXIDE; HYDROQUINONES; IRON; MASS SPECTROMETRY; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; MULTIGENE FAMILY; OPEN READING FRAMES; OXYGENASES; PARABENS; PHENANTHROLINES; PROTEIN SUBUNITS; PSEUDOMONAS FLUORESCENS; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; TEMPERATURE;

PSEUDOMONAS FLUORESCENS;

EID: 48149092978     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01945-07     Document Type: Article

References (83)

1. Altschul, S. F., T. L. Madden, A. A. Schaeffer, J. Zhang, Z. Zhang, W. Miller, and D. J. Lipman. 1997. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25:3389-3402.
2. 2+ environment. J. Biol. Chem. 258:14981-14991.
3. Arias-Barrau, E., E. R. Olivera, J. M. Luengo, C. Fernandez, B. Galan, J. L. Garcia, E. Diaz, and B. Minambres. 2004. The homogentisate pathway: a central catabolic pathway involved in the degradation of L- phenylalanine, L-tyrosine, and 3-hydroxyphenylacetate in Pseudomonas putida. J. Bacteriol. 186:5062-5077.
4. Armengaud, J., K. N. Timmis, and R. M. Wittich. 1999. A functional 4-hydroxysalicylate/hydroxyquinol degradative pathway gene cluster is linked to the initial dibenzo-p-dioxin pathway genes in Sphingomonas sp. strain RW1. J. Bacteriol. 181:3452-3461.
5. Bang, S.-W., and G. J. Zylstra. 1997. Cloning and sequencing of the hydroquinone 1,2-dioxygenase, γ-hydroxymuconic semialdehyde dehydrogenase, maleylacetate reductase genes from Pseudomonas fluorescens ENV2030, abstr. Q-383, p.519. Abstr. 97th Gen. Meet. Am. Soc. Microbiol. American Society for Microbiology, Washington, DC.
6. Bertini, I., F. Briganti, S. Mangani, H. F. Nolting, and A. Scozzafava. 1995. Biophysical investigation of bacterial aromatic extradiol dioxygenases involved in biodegradation processes. Coord. Chem. Rev. 144:321-345.
7. Boldt, Y. R., M. J. Sadowsky, L. B. Ellis, L. Que, Jr., and L. P. Wackett. 1995. A manganese-dependent dioxygenase from Arthrobacter globiformis CM-2 belongs to the major extradiol dioxygenase family. J. Bacteriol. 177:1225-1232.
8. Boyington, J. C., B. J. Gaffney, and L. M. Amzel. 1993. The three-dimensional structure of an arachidonic acid 15-lipoxygenase. Science 260:1482-1486.
9. Cai, M., and L. Xun. 2002. Organization and regulation of pentachlorophenol-degrading genes in Sphingobium chlorophenolicum ATCC 39723. J. Bacteriol. 184:4672-4680.
10. Cain, R. B., P. Fortnagel, S. Hebenbrock, G. W. Kirby, H. J. McLenaghan, G. V. Rao, and S. Schmidt. 1997. Biosynthesis of a cyclic tautomer of (3-methylmaleyl)acetone from 4-hydroxy-3,5-dimethylbenzoate by Pseudomonas sp. HH35 but not by Rhodococcus rhodochrous N75. Biochem. Biophys. Res. Commun. 238:197-201.
11. 2+. Biochim. Biophys. Acta 1596:283-292.
12. Cavanagh, J., R. Thompson, B. Bobay, L. M. Benson, and S. Naylor. 2002. Stoichiometries of protein-protein/DNA binding and conformational changes for the transition-state regulator AbrB measured by pseudo cell-size exclusion chromatography-mass spectrometry. Biochemistry 41:7859-7865.
13. Chapman, P. J., and D. J. Hopper. 1968. The bacterial metabolism of 2,4-xylenol. Biochem. J. 110:491-498.
14. Chauhan, A., A. K. Chakraborti, and R. K. Jain. 2000. Plasmid-encoded degradation of p-nitrophenol and 4-nitrocatechol by Arthrobacter protophormiae. Biochem. Biophys. Res. Commun. 270:733-740.
15. Chauhan, A., S. K. Samanta, and R. K. Jain. 2000. Degradation of 4-nitrocatechol by Burkholderia cepacia: a plasmid-encoded novel pathway. J. Appl. Microbiol. 88:764-772.
16. Cripps, R. E. 1975. The microbial metabolism of acetophenone. Metabolism of acetophenone and some chloroacetophenones by an Arthrobacter species. Biochem. J. 152:233-241.
17. Cripps, R. E., P. W. Trudgill, and J. G. Whateley. 1978. The metabolism of 1-phenylethanol and acetophenone by Nocardia T5 and an Arthrobacter species. Eur. J. Biochem. 86:175-186.
18. Curti, B., S. Ronchi, U. Branzoli, G. Ferri, and C. H. Williams, Jr. 1973. Improved purification, amino acid analysis and molecular weight of homogenous D-amino acid oxidase from pig kidney. Biochim. Biophys. Acta 327: 266-273.
19. Darby, J. M., D. G. Taylor, and D. J. Hopper. 1987. Hydroquinone as the ring-fission substrate in the catabolism of 4-ethylphenol and 4-hydroxyacetophenone by Pseudomonas putida JD1. J. Gen. Microbiol. 133:2137-2146.
20. Daubaras, D. L., K. Saido, and A. M. Chakrabarty. 1996. Purification of hydroxyquinol 1,2-dioxygenase and maleylacetate reductase: the lower pathway of 2,4,5-trichlorophenoxyacetic acid metabolism by Burkholderia cepacia AC1100. Appl. Environ. Microbiol. 62:4276-4279.
21. Eppink, M. H. M., S. A. Boeren, J. Vervoort, and W. J. H. van Berkel. 1997. Purification and properties of 4-hydroxybenzoate 1-hydroxylase (decarboxylating), a novel flavin adenine dinucleotide-dependent monooxygenase from Candida parapsilosis CBS604. J. Bacteriol. 179:6680-6687.
22. Ferraroni, M., J. Seifert, V. M. Travkin, M. Thiel, S. Kaschabek, A. Scozzafava, L. Golovleva, M. Schlömann, and F. Briganti. 2005. Crystal structure of the hydroxyquinol 1,2-dioxygenase from Nocardioides simplex 3E, a key enzyme involved in polychlorinated aromatics biodegradation. J. Biol. Chem. 280:21144-21154.
23. Flo, T. H., K. D. Smith, S. Sato, D. J. Rodriguez, M. A. Holmes, R. K. Strong, S. Akira, and A. Aderem. 2004. Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron. Nature 432:917-921.
24. Goa, J. 1953. A micro biuret method for protein determination. Determination of total protein in cerebrospinal fluid. Scan. J. Clin. Lab. Investig. 5:218-222.
25. Göbel, M., O. H. Kranz, S. R. Kaschabek, E. Schmidt, D. H. Pieper, and W. Reineke. 2004. Microorganisms degrading chlorobenzene via a meta-cleavage pathway harbor highly similar chlorocatechol 2,3-dioxygenase-encoding gene clusters. Arch. Microbiol. 182:147-156.
26. Hall, T. A. 1999. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp. Ser. 41:95-98.
27. Hanne, L. F., L. L. Kirk, S. M. Appel, A. D. Narayan, and K. K. Bains. 1993. Degradation and induction specificity in Actinomycetes that degrade p-nitrophenol. Appl. Environ. Microbiol. 59:3505-3508.
28. Harpel, M. R., and J. D. Lipscomb. 1990. Gentisate 1,2-dioxygenase from Pseudomonas. Purification, characterization, and comparison of the enzymes from Pseudomonas testosteroni and Pseudomonas acidovorans. J. Biol. Chem. 265:6301-6311.
29. 2+ and mechanism of turnover. J. Biol. Chem. 265:22187-22196.
30. Havel, J., and W. Reineke. 1993. Microbial degradation of chlorinated acetophenones. Appl. Environ. Microbiol. 59:2706-2712.
31. Higson, F. K., and D. D. Focht. 1990. Bacterial degradation of ring-chlorinated acetophenones. Appl. Environ. Microbiol. 56:3678-3685.
32. Hopper, D. J., H. G. Jones, E. A. Elmorsi, and M. E. Rhodes-Roberts. 1985. The catabolism of 4-hydroxyacetophenone by an Alcaligenes sp. J. Gen. Microbiol. 131:1807-1814.
33. Hugo, N., J. Armengaud, J. Gaillard, K. N. Timmis, and Y. Jouanneau. 1998. A novel [2Fe-2S] ferredoxin from Pseudomonas putida mt2 promotes the reductive reactivation of catechol 2,3-dioxygenase. J. Biol. Chem. 273:9622-9629.
34. Hugo, N., C. Meyer, J. Armengaud, J. Gaillard, K. N. Timmis, and Y. Jouanneau. 2000. Characterization of three XylT-like [2Fe-2S] ferredoxins associated with catabolism of cresols or naphthalene: evidence for their involvement in catechol dioxygenase reactivation. J. Bacteriol. 182:5580-5585.
35. Jain, R. K., J. H. Dreisbach, and J. C. Spain. 1994. Biodegradation of p-nitrophenol via 1,2,4-benzenetriol by an Arthrobacter sp. Appl. Environ. Microbiol. 60:3030-3032.
36. Kamerbeek, N. M., D. B. Janssen, W. J. H. van Berkel, and M. W. Fraaije. 2003. Baeyer-Villiger monooxygenases, an emerging family of flavin-dependent biocatalysts. Adv. Synth. Catal. 345:667-678.
37. Kamerbeek, N. M., M. J. H. Moonen, J. G. M. van der Ven, W. J. H. van Berkel, M. W. Fraaije, and D. B. Janssen. 2001. 4-Hydroxyacetophenone monooxygenase from Pseudomonas fluorescens ACB. A novel flavoprotein catalyzing Baeyer-Villiger oxidation of aromatic compounds. Eur. J. Biochem. 268:2547-2557.
38. Kamerbeek, N. M., A. J. Olsthoorn, M. W. Fraaije, and D. B. Janssen. 2003. Substrate specificity and enantioselectivity of 4-hydroxyacetophenone monooxygenase. Appl. Environ. Microbiol. 69:419-426.
39. Latus, M., H. Seitz, J. Eberspacher, and F. Lingens. 1995. Purification and characterization of hydroxyquinol 1,2-dioxygenase from Azotobacter sp. strain GP1. Appl. Environ. Microbiol. 61:2453-2460.
40. Lendenmann, U., and J. C. Spain. 1996. 2-aminophenol 1,6-dioxygenase: a novel aromatic ring cleavage enzyme purified from Pseudomonas pseudoalcaligenes JS45. J. Bacteriol. 178:6227-6232.
41. Lipscomb, J. D., and A. M. Orville. 1992. Mechanistic aspects of dihydroxybenzoate dioxygenases, p. 243-298. In H. Sigel and A. Sigel (ed.), Degradation of environmental pollutants by microorganisms and their metalloenzymes. Metal ions in biological systems, vol. 28. Dekker, New York, NY.
42. Middelhoven, W. J., A. Coenen, B. Kraakman, and M. D. Sollewijn Gelpke. 1992. Degradation of some phenols and hydroxybenzoates by the imperfect ascomycetous yeasts Candida parapsilosis and Arxula adeninivorans: evidence for an operative gentisate pathway. Antonie van Leeuwenhoek 62:181-187.
43. Minor, W., J. Steczko, J. T. Bolin, Z. Otwinowski, and B. Axelrod. 1993. Crystallographic determination of the active site iron and its ligands in soybean lipoxygenase L-1. Biochemistry 32:6320-6323.
44. Miyauchi, K., Y. Adachi, Y. Nagata, and M. Takagi. 1999. Cloning and sequencing of a novel meta-cleavage dioxygenase gene whose product is involved in degradation of γ-hexachlorocyclohexane in Sphingomonas paucimobilis. J. Bacteriol. 181:6712-6719.
45. Moonen, M. J. H., M. W. Fraaije, I. M. C. M. Rietjens, C. Laane, and W. J. H. Van Berkel. 2002. Flavoenzyme-catalyzed oxygenations and oxidations of phenolic compounds. Adv. Synth. Catal. 344:1023-1035.
46. Moonen, M. J. H., N. M. Kamerbeek, A. H. Westphal, S. A. Boeren, D. B. Janssen, M. W. Fraaije, and W. J. H. Van Berkel. 2008. Elucidation of the
47. 4-hydroxyacetophenone catabolic pathway in Pseudomonas fluorescens ACB. J. Bacteriol. 190:5190-5198.
48. 19F NMR study on the biological Baeyer-Villiger oxidation of acetophenones. J. Ind. Microbiol. Biotechnol. 26:35-42.
49. Moonen, M. J. H., A. H. Westphal, I. M. C. M. Rietjens, and W. J. H. Van Berkel. 2005. Enzymatic Baeyer-Villiger oxidation of benzaldehydes. Adv. Synth. Catal. 347:1027-1034.
50. Muraki, T., M. Taki, Y. Hasegawa, H. Iwaki, and P. C. Lau. 2003. Prokaryotic homologs of the eukaryotic 3-hydroxyanthranilate 3,4-dioxygenase and 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase in the 2-nitrobenzoate degradation pathway of Pseudomonas fluorescens strain KU-7. Appl. Environ. Microbiol. 69:1564-1572.
51. Nakai, C., T. Nakazawa, and M. Nozaki. 1988. Purification and properties of catechol 1,2-dioxygenase (pyrocatechase) from Pseudomonas putida mt-2 in comparison with that from Pseudomonas arvilla C-1. Arch. Biochem. Biophys. 267:701-713.
52. Ohtsubo, Y., K. Miyauchi, K. Kanda, T. Hatta, H. Kiyohara, T. Senda, Y. Nagata, Y. Mitsui, and M. Takagi. 1999. PcpA, which is involved in the degradation of pentachlorophenol in Sphingomonas chlorophenolica ATCC 39723, is a novel type of ring-cleavage dioxygenase. FEBS Lett. 459:395-398.
53. Page, R. D. M. 1996. TREEVIEW: An application to display phylogenetic trees on personal computers. Comput. Appl. Biosci. 12:357-358.
54. Polissi, A., and S. Harayama. 1993. In vivo reactivation of catechol 2,3-dioxygenase mediated by a chloroplast-type ferredoxin: a bacterial strategy to expand the substrate specificity of aromatic degradative pathways. EMBO J. 12:3339-3347.
55. Que, L. J., and R. Y. N. Ho. 1996. Dioxygen activation by enzymes with mononuclear non-heme iron active sites. Chem. Rev. 96:2607-2624.
56. Rieble, S., D. K. Joshi, and M. H. Gold. 1994. Purification and characterization of a 1,2,4-trihydroxybenzene 1,2-dioxygenase from the basidiomycete Phanerochaete chrysosporium. J. Bacteriol. 176:4838-4844.
57. Roach, P. L., I. J. Clifton, V. Fulop, K. Harlos, G. J. Barton, J. Hajdu, I. Andersson, C. J. Schofield, and J. E. Baldwin. 1995. Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes. Nature 375:700-704.
58. Rosenfeld, J., J. Capdevielle, J. C. Guillemot, and P. Ferrara. 1992. In-gel digestion of proteins for internal sequence analysis after one- or two-dimensional gel electrophoresis. Anal. Biochem. 203:173-179.
59. Sato, N., Y. Uragami, T. Nishizaki, Y. Takahashi, G. Sazaki, K. Sugimoto, T. Nonaka, E. Masai, M. Fukuda, and T. Senda. 2002. Crystal structures of the reaction intermediate and its homologue of an extradiol-cleaving catecholic dioxygenase. J. Mol. Biol. 321:621-636.
60. Schmidt, A., U. Bahr, and M. Karas. 2001. Influence of pressure in the first pumping stage on analyte desolvation and fragmentation in nano-ESI MS. Anal. Chem. 73:6040-6046.
61. Schmidt, S., and G. W. Kirby. 2001. Dioxygenative cleavage of C-methylated hydroquinones and 2,6-dichlorohydroquinone by Pseudomonas sp. HH35. Biochim. Biophys. Acta 1568:83-89.
62. Shevchenko, A., M. Wilm, O. Vorm, and M. Mann. 1996. Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal. Chem. 68:850-858.
63. Sobott, F., H. Hernandez, M. G. McCammon, M. A. Tito, and C. V. Robinson. 2002. A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies. Anal. Chem. 74:1402-1407.
64. Spain, J. C., and D. T. Gibson. 1991. Pathway for biodegradation of p-nitrophenol in a Moraxella sp. Appl. Environ. Microbiol. 57:812-819.
65. Steiner, R. A., K. H. Kalk, and B. W. Dijkstra. 2002. Anaerobic enzyme substrate structures provide insight into the reaction mechanism of the copper-dependent quercetin 2,3-dioxygenase. Proc. Natl. Acad. Sci. USA 99:16625-16630.
66. Sugimoto, K., T. Senda, H. Aoshima, E. Masai, M. Fukuda, and Y. Mitsui. 1999. Crystal structure of an aromatic ring opening dioxygenase LigAB, a protocatechuate 4,5-dioxygenase, under aerobic conditions. Structure 7:953-965.
67. Sze, I. S., and S. Dagley. 1984. Properties of salicylate hydroxylase and hydroxyquinol 1,2-dioxygenase purified from Trichosporon cutaneum. J. Bacteriol. 159:353-359.
68. Tahallah, N., M. Pinkse, C. S. Maier, and A. J. Heck. 2001. The effect of the source pressure on the abundance of ions of noncovalent protein assemblies in an electrospray ionization orthogonal time-of-flight instrument. Rapid. Commun. Mass Spectrom. 15:596-601.
69. Takenaka, S., S. Murakami, R. Shinke, K. Hatakeyama, H. Yukawa, and K. Aoki. 1997. Novel genes encoding 2-aminophenol 1,6-dioxygenase from Pseudomonas species AP-3 growing on 2-aminophenol and catalytic properties of the purified enzyme. J. Biol. Chem. 272:14727-14732.
70. Thompson, J. D., D. G. Higgins, and T. J. Gibson. 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.
71. Titus, G. P., H. A. Mueller, J. Burgner, S. Rodriguez De Cordoba, M. A. Penalva, and D. E. Timm. 2000. Crystal structure of human homogentisate dioxygenase. Nat. Struct. Biol. 7:542-546.
72. Tropel, D., C. Meyer, J. Armengaud, and Y. Jouanneau. 2002. Ferredoxin-mediated reactivation of the chlorocatechol 2,3-dioxygenase from Pseudomonas putida GJ31. Arch. Microbiol. 177:345-351.
73. van Baal, I., H. Malda, S. A. Synowsky, J. L. van Dongen, T. M. Hackeng, M. Merkx, and E. W. Meijer. 2005. Multivalent peptide and protein dendrimers using native chemical ligation. Angew. Chem. Int. Ed. Engl. 44:5052-5057.
74. van Berkel, W. J. H., A. H. Westphal, K. Eschrich, M. H. M. Eppink, and A. de Kok. 1992. Substitution of Arg214 at the substrate-binding site of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Eur. J. Biochem. 210:411-419.
75. van den Heuvel, R. H., E. van Duijn, H. Mazon, S. A. Synowsky, K. Lorenzen, C. Versluis, S. J. Brouns, D. Langridge, J. van der Oost, J. Hoyes, and A. J. Heck. 2006. Improving the performance of a quadrupole time-of-flight instrument for macromolecular mass spectrometry. Anal. Chem. 78:7473-7483.
76. Vetting, M. W., L. P. Wackett, L. Que, Jr., J. D. Lipscomb, and D. H. Ohlendorf. 2004. Crystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases. J. Bacteriol. 186:1945-1958.
77. Weber, K., and M. Osborn. 1969. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem. 244:4406-4412.
78. Westphal, A. H., and A. de Kok. 1988. Lipoamide dehydrogenase from Azotobacter vinelandii. Molecular cloning, organization and sequence analysis of the gene. Eur. J. Biochem. 172:299-305.
79. Whiting, A. K., Y. R. Boldt, M. P. Hendrich, L. P. Wackett, and L. Que, Jr. 1996. Manganese(II)-dependent extradiol-cleaving catechol dioxygenase from Arthrobacter globiformis CM-2. Biochemistry 35:160-170.
80. Wolgel, S. A., J. E. Dege, P. E. Perkins-Olson, C. H. Jaurez-Garcia, R. L. Crawford, E. Munck, and J. D. Lipscomb. 1993. Purification and characterization of protocatechuate 2,3-dioxygenase from Bacillus macerans: a new extradiol catecholic dioxygenase. J. Bacteriol. 175:4414-4426.
81. Xu, L., K. Resing, S. L. Lawson, P. C. Babbitt, and S. D. Copley. 1999. Evidence that pcpA encodes 2,6-dichlorohydroquinone dioxygenase, the ring cleavage enzyme required for pentachlorophenol degradation in Sphingomonas chlorophenolica strain ATCC 39723. Biochemistry 38:7659-7669.
82. Xun, L., J. Bohuslavek, and M. Cai. 1999. Characterization of 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA) of Sphingomonas chlorophenolica ATCC 39723. Biochem. Biophys. Res. Commun. 266:322-325.
83. Zylstra, G. J., S.-W. Bang, L. M. Newman, and L. L. Perry. 2000. Microbial degradation of mononitrophenols and mononitrobenzoates, p. 145-160. In J. C. Spain, J. B. Hughes, and H.-J. Knackmuss (ed.), Biodegradation of nitroaromatic compounds and explosives. CRC Press, Boca Raton, FL.