Catechol 1,2-dioxygenase from the new aromatic compounds - Degrading Pseudomonas putida strain N6

International Biodeterioration and Biodegradation

Volumn 65, Issue 3, 2011, Pages 504-512

  Guzik, Urszula ^a   Greń, Izabela ^a   Hupert Kocurek, Katarzyna ^a   Wojcieszyńska, Danuta ^a  

^a UNIVERSITY OF SILESIA   (Poland)

Author keywords

Aromatic compounds; Biodegradation; Dioxygenases; Pseudomonas

Indexed keywords

16S RDNA SEQUENCE; 4-HYDROXYBENZOIC ACIDS; ACTIVATED SLUDGE; AROMATIC SUBSTRATES; BENZOIC ACID; BIOCHEMICAL CHARACTERISTICS; DIOXYGENASES; ENERGY SOURCE; GRAM-NEGATIVE BACTERIA; HIGH ACTIVITY; KINETIC STUDY; NUCLEOTIDE SEQUENCES; PHYLOGENETIC ANALYSIS; PROTOCATECHUATE; PSEUDOMONAS; PSEUDOMONAS PUTIDA; PSEUDOMONAS PUTIDA STRAIN; SOLE CARBON; WIDE SPECTRUM;

ACTIVATED SLUDGE PROCESS; AROMATIZATION; BACTERIA; BIODEGRADATION; DEGRADATION; ENZYMES; GENE ENCODING; MICROBIOLOGY; PH EFFECTS; SEWAGE; SEWAGE TREATMENT PLANTS; STRAIN;

PHENOLS;

ACTIVATED SLUDGE; BACTERIUM; BIODEGRADATION; CARBON; ENERGY; ENZYME ACTIVITY; MORPHOLOGY; PHYLOGENETICS; PHYSICOCHEMICAL PROPERTY; SAMPLING; SUBSTRATE;

POLAND;

NEGIBACTERIA; PSEUDOMONAS; PSEUDOMONAS PUTIDA;

EID: 79953107665     PISSN: 09648305     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ibiod.2011.02.001     Document Type: Article

References (55)

1. Adebusoye S.A., Picardal F.W., Ilori M.O., Amund O.O., Fuqua C., Grindle N. Aerobic degradation of di- and trichlorobenzenes by two bacteria isolated from polluted tropical soils. Chemosphere 2007, 66:1939-1946.
2. Albaugh C.E. Degradation of monoaromatic compounds by an aerobic halotolerant alkaliphilic bacterium 2005, Washington State University, Washington, USA.
3. Alvarez-Rodriguez M.L., Belloch C., Villa M., Uruburu F., Lariba G., Coque J.J.R. Degradation of vanillic acid and production of guaiacol microorganisms isolated from cork samples. FEMS Microbiology Letters 2003, 220:40-55.
4. Beil S., Timmis K.N., Pieper D.H. Genetic and biochemical analyses of the tec operon suggest a route for evolution of chlorobenzene degradation genes. Journal of Bacteriology 1999, 181:341-346.
5. Borowski T., Siegbahn E.M. Mechanism for catechol ring cleavage by non-heme iron intradiol dioxygenases: a hybryd DFT study. Journal of the American Chemical Society 2006, 128:12941-12953.
6. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 1976, 72:248-258.
7. Briganti F., Pessione E., Giunta C., Mazzoli R., Scozzafava A. Purification and catalytic properties of two catechol 1,2-dioxygenase isozymes from benzoate-grown cells of Acinetobacter radioresistens. Journal of Protein Chemistry 2000, 19:709-716.
8. Bruijnincx P.C.A., van Koten G., Gebbink R.J.M.K. Mononuclear non-heme iron enzymes with the 2-His-1-carboxylate facial triad: recent development in enzymology and modeling studies. Chemical Society Reviews 2008, 37:2716-2744.
9. Buchan A., Collier L.S., Neidle E.L., Moran M.A. Key aromatic-ring-cleaving enzyme, protocatechuate 3,4-dioxygenase, in the ecologically important marine Roseobacter lineage. Applied and Environmental Microbiology 2000, 66:4662-4672.
10. Bugg T.D.H. Dioxygenase enzymes: catalytic mechanisms and chemical models. Tetrahedron 2003, 59:7075-7101.
11. Bugg T.D.H., Ramaswamy S. Non-heme iron-dependent dioxygenases: unraveling catalytic mechanism for complex enzymatic oxidation. Current Opinion in Chemical Biology 2008, 12:134-140.
12. Bugg T.D.H., Lin G. Solving the riddle of the intradiol and extradiol catechol dioxygenases: how do enzymes control hydroperoxide rearrangements?. Chemical Communications 2001, 941-952.
13. Chae J.Ch., Kim E., Bini E., Zylstra G.J. Comparative analysis of the catechol 2,3-dioxygenase gene locus in thermoacidophilic archeon Sulfolobus solfataricus strain 98/2. Biochemical and Biophysical Research Communications 2007, 357:815-819.
14. Chow K.T., Pope M.T., Davies J. Characterization of a vanillic acid non-oxidative decarboxylation gene cluster from Streptomyces sp. D7. Microbiology 1999, 145:2393-2403.
15. Chung T.P., Wu Ch, Juang R.S. Improved dynamic analysis on cell growth with substrate inhibition using two-phase models. Biochemical Engineering Journal 2005, 25:209-217.
16. Costas M., Mehn M.P., Jensen M.P., Que L. Dioxygen activation at mononuclear nonheme iron active sites: enzymes, models, and intermediates. Chemical Reviews 2004, 104:939-986.
17. Earhart C.A., Vetting M.W., Gosu R., Michaud-Soret I., Que L., Ohlendorf D.H. Structure of catechol 1,2-dioxygenase from Pseudomonas arvilla. Biochemical and Biophysical Research Communications 2005, 338:198-205.
18. Fujisawa H., Hayaishi O. Protocatechuate 3,4-dioxygenase - crystallization and characterization. Journal of Biological Chemistry 1968, 243:2673-2681.
19. Furukawa H., Morita H., Yoshida T., Nagasawa T. Conversion of isoeugenol into vanilic acid by Pseudomonas putida 158 cells exhibiting high isoeugenol-degrading activity. Journal of Bioscience and Bioengineering 2003, 96:401-403.
20. Giedraityte G., Kalediene L. Catechol 1,2-dioxygenase from α-naphtol degrading thermophilic Geobacillus sp. strain: purification and properties. Central European Journal of Biology 2009, 4:68-73.
21. Glucksman A.M., Skipper H.D., Brigmon R.L., Santo Domingo J.W. Use of the MIDI-FAME technique to characterize groundwater communities. Journal of Applied Microbiology 2000, 88:711-719.
22. Greń I., Wojcieszyńska D., Guzik U., Perkosz M., Hupert-Kocurek K. Enhanced biotransformation of mononitrophenols by Stenotrophomonas maltophilia KB2 in the presence of aromatic compounds of plant origin. World Journal of Microbiology and Biotechnology 2010, 26:289-295.
23. Guzik U., Greń I., Wojcieszyńska D., Łabużek S. Isolation and characterization of a novel strain of Stenotrophomonas maltophilia possessing various dioxygenases for monocyclic hydrocarbon degradation. Brazilian Journal of Microbiology 2009, 40:285-291.
24. Harwood C.S., Parales R.E. The β-ketoadipate pathway and the biology of self-identity. Annual Review of Microbiology 1996, 50:553-590.
25. Hatta T., Mukerjee-Dhar G., Damborsky J., Kiyohara H., Kimbara K. Characterization of a novel thermostable Mn(II)-dependent 2,3-dihydroxybiphenyl 1,2-dioxyegnase from a PCB and naphthalene-degrading Bacillus sp. JF8. Journal of Biological Chemistry 2003, 278:21483-21492.
26. Holt J.G., Krieg N.R., Sneath P.H.A., Staley J.T., Williams S.T. Bergey's manual of determinative bacteriology 1994, Williams and Wilkins, USA.
27. Kukor J.J., Olsen R.H. Catechol 2,3-dioxygenases functional in oxygen-limited (hypoxic) environments. Applied and Environmental Microbiology 1996, 62:1728-1740.
28. Lillis L., Clipson N., Doyle E. Quantification of catechol dioxygenase gene expression in soil during degradation of 2,4-dichlorophenol. FEMS Microbiology Ecology 2010, 73:363-369.
29. Lonergan D.J., Jenter H.L., Coates J.D., Phillips E.J., Schmidt T.M., Lovley D.R. Phylogenetic analysis of dissimilatory Fe (III) - reducing bacteria. Journal of Bacteriology 1996, 178:2402-2408.
30. Mars A.E., Kingman J., Kaschabek S.R., Reineke W., Janssen D.B. Conversion of 3-chlorocatechol by various catechol 2,3-dioxygenases and sequence analysis of the chlorocatechol dioxygenase region of Pseudomonas putida GJ31. Journal of Bacteriology 1999, 181:1309-1318.
31. Masai E., Shinohara S., Hara H., Nishikawa S., Katayama R., Fukuda M. Genetic and biochemical characterization of a 2-pyrone-4,6- dicarboxylic acid hydrolase involved in the protocatechuate 4,5-cleavage pathway of Sphingomonas paucimobilis SYK-6. Journal of Bacteriology 1999, 181:55-62.
32. Matthew W., Vetting M.W., Douglas H., Ohlendorf D.H. The 1.8 Å crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker. Structure 2008, 8:429-440.
33. Melo F.A., Araujo A.P.U., Costa-Filho A.J. Role of cis, cis-muconic acid in the catalysis of Pseudomonas putida chlorocatechol 1,2-dioxygenase. International Journal of Biological Macromolecules 2010, 47:233-237.
34. Miguez C.B., Greer Ch.W., Ingram J.M. Purification and properties of chlorocatechol 1,2-dioxygenase from Alcaligenes denitrificans BRI 6011. Canadian Journal of Microbiology 1992, 39:1-5.
35. Miller A.F. The shortes wire. Proceedings of the National Academy of Sciences of the United States of America 2008, 105:7341-7342.
36. Mishira V., Lal R., Srinivasa N. Enzymes and operons mediating xenobiotic degradation in bacteria. Critical Review of Microbiology 2001, 27:133-166.
37. Moiseeva O.V., Belova O.V., Solyanikova I.P., Schlomann M., Golovleva L.A. Enzymes of a new modified ortho-pathway utilizing 2-chlorophenol in Rhodococcus opacus 1CP. Biochemistry 2001, 66:548-555.
38. Nakai Ch., Horiike K., Kuramitsug S., Kagamiyamap H., Nozaki M. Three isozymes of catechol l,2-dioxygenase (Pyrocatechase), from Pseudomonas arvilla C-l. Journal of Biological Chemistry 1990, 265:660-665.
39. Neidle E.L., Hartnett Ch., Bonitz S., Ornston L.N. DNA sequence of the Acinetobacter calcoaceticus catechol 1,2-dioxygenase I structural gene catA: evidence for evolutionary divergence of intradiol dioxygenases by acquisition of DNA sequence repetitions. Journal of Bacteriology 1998, 170:4874-4880.
40. Ohlendorf D.H., Orville A.M., Lipscomb J.D. Structure of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa at 2.15 Å resolution. Journal of Molecular Biology 1994, 244:586-608.
41. 3+ ligand displacement in response to substrate binding. Biochemistry 1997, 36:10052-10066.
42. Palaniandavar M., Velusamy M., Mayilmurugan R. Iron(III) complexes of certain tetradentate phenolate ligands as functional models for catechol dioxygenases. Journal of Chemical Science 2006, 118:601-610.
43. Sambrook J., Fritsch E.F., Maniatis T. Molecular cloning: a laboratory manual 1989, Cold Spring Harbor Laboratory Press, New York. second ed.
44. Sasser, M., 1990. Technical note # 101-10.
45. Sauret-Ignazi G., Gagnon J., Beguin C., Barrelle M., Markowicz Y., Pelmont J. Characterization of a chromosomally encoded catechol 1,2-dioxygenase (E.C.1.13.11.1) from Alcaligenes eutrophus Ch34. Archives of Microbiology 1996, 166:42-50.
46. Saxena P., Thakur I.S. Purification and characterization of catechol 1,2-dioxygenase of Pseudomonas fluorescens for degradation of 4-chlorobenzoic acid. Indian Journal of Biotechnology 2005, 4:134-138.
47. Sei K., Asano K., Tateishi N., Mori K., Ike M., Fujita M. Design of PCR primers and gene probes for the general detection of bacterial populations capable of degrading aromatic compounds via catechol cleavage pathways. Journal of Bioscience and Bioengineering 1999, 88:542-550.
48. Song J., Sung J., Kim Y.M., Zylstra G.J., Kim E. Roles of the meta- and the ortho-cleavage pathways for the efficient utilization of aromatic hydrocarbons by Sphingomonas yanoikuyae B1. Journal of Microbiology 2000, 38:245-249.
49. Strachan P.D., Freer A.A., Fewson Ch.A. Purification and characterization of catechol 1,2-dioxygenase from Rhodococcus rhodochrous NCIMB 13259 and cloning and sequencing of its catA gene. Biochemical Journal 1998, 333:741-747.
50. Teramoto H., Tanaka H., Wariishi H. Degradation of 4-nitrophenol by the lignin-degrading basidiomycete Phanerochaete chrysosporium. Applied Microbiology and Biotechnology 2004, 66:312-317.
51. Vaillancourt F.H., Bolin J.T., Eltis L.D. The Ins and Outs of ring-cleaving dioxygenases. Critical Reviews in Biochemistry and Molecular Biology 2006, 41:241-267.
52. Vetting M.W., Ohlendorf D.H. The 1.8 Å crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker. Structure 2000, 8:429-440.
53. Wang Ch.L., You S.L., Wang S.L. Purification and characterization of a novel catechol 1,2-dioxygenase from Pseudomonas aeruginosa with benzoic acid as a carbon source. Process Biochemistry 2006, 41:1594-1601.
54. Wojcieszynska D., Guzik U., Greń I., Perkosz M., Hupert-Kocurek K. Induction of aromatic ring - cleavage dioxygenases in Stenotrophomonas maltophilia strain KB2 in cometabolic systems. World Journal of Microbiology and Biotechnology 2010, 10.1007/s11274-010-0520-6.
55. Zeyaullah M., Abdelkafe A.S., Zabya W.B., Ali A. Biodegradation of catechols by micro-organisms - a short review. African Journal of Biotechnology 2009, 8:2916-2922.