Purification and characterization of a novel naphthalene dioxygenase from Rhodococcus sp. strain NCIMB12038

Journal of Bacteriology

Volumn 181, Issue 19, 1999, Pages 6200-6204

  Larkin, Michael J ^a   Allen, Christopher C R ^b   Kulakov, Leonid A ^b   Lipscomb, David A ^b  

^a QUEEN'S UNIVERSITY BELFAST   (United Kingdom)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; NAPHTHALENE DERIVATIVE; OXYGENASE;

AMINO ACID SEQUENCE; ARTICLE; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME SUBUNIT; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PSEUDOMONAS PUTIDA; RHODOCOCCUS; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY;

ACTINOBACTERIA (CLASS); BACTERIA (MICROORGANISMS); PSEUDOMONAS; PSEUDOMONAS PUTIDA; RHODOCOCCUS; RHODOCOCCUS SP.; UNCULTURED ACTINOMYCETE;

EID: 0032819205     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.19.6200-6204.1999     Document Type: Article

References (25)

1. Allen, C. C. R., D. R. Boyd, M. J. Larkin, K. A. Reid, N. D. Sharma, and K. Wilson. 1997. Metabolism of naphthalene, 1-naphthol, indene, and indole by Rhodococcus sp. strain NCIMB 12038. Appl. Environ. Microbiol. 63:151-155.
2. Butler, C. S., and J. R. Mason. 1997. Structure-function analysis of the bacterial aromatic ring-hydroxylating dioxygenases. Adv. Microb. Physiol. 38:47-84.
3. Cerniglia, C. E. 1992. Biodegradation of polycyclic aeromatic hydrocarbons. Biodegradation 3:351-368.
4. Ensley. B. D., and D. T. Gibson. 1983. Naphthalene dioxygenase: purification and properties of a terminal oxygenase component. J. Bacteriol. 155:505-511.
5. Ensley, B. D., D. T. Gibson, and A. L. Laborde. 1982. Oxidation of naphthalene by a multi-component enzyme system from Pseudomonas sp. strain NCIB 9816. J. Bacteriol. 149:948-954.
6. Finnerty, W. R. 1992. The biology and genetics of the genus Rhodococcus. Annu. Rev. Microbiol. 46:193-218.
7. Grund, E., B. Denecke, and R. Eichenlaub. 1992. Naphthalene degradation via salicylate and gentisate by Rhodococcus sp. strain B4. Appl. Environ. Microbiol. 58:1874-1877.
8. NAP reductase, a component of naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816. J. Bacteriol. 172:457-464.
9. Harayama, S., M. Kok, and E. L. Niedle. 1992. Functional and evolutionary relationships among diverse oxygenases. Annu. Rev. Microbiol. 46:565-601.
10. Iwasaki, T., Y. Isogai, T. Iizuka, and T. Oshima. 1995. Sulredoxin: a novel iron-sulfur protein of the thermoacidophilic archaeon Sulfolobus sp. strain 7 with a Rieske-type [2Fe-2S] center. J. Bacteriol. 177:2576-2582.
11. Jeffrey, A. M., H. J. C. Yeh, D. M. Jerina, T. R. Patel, J. F. Davey, and D. T. Gibson. 1975. Initial reactions in the oxidation of naphthalene by Pseudomonas putida. Biochemistry 14:575-584.
12. Kauppi, B., K. Lee, E. Carrendano, R. E. Parales, D. T. Gibson, H. Eklund, and S. Ramaswamy. 1998. Structure of an aromatic-ring-hydroxylating di-oxygenase - naphthalene 1,2-dioxygenase. Structure 6:571-586.
13. Kulakova, A. N., T. M. Stafford, M. J. Larkin, and L. A. Kulakov. 1995. Plasmid pRTL1 controlling 1-chloroalkane degradation by Rhodococcus rhodochrous NCIMB13064. Plasmid 33:208-217.
14. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
15. Larkin, M. J., and M. J. Day. 1986. The metabolism of carbaryl by three isolates, Pseudomonas spp (NCIB12042 and 12043) and Rhodococcus sp (NCIB12038), from garden soil. J. Appl. Bacteriol. 60:233-242.
16. Latimer, M. T., M. H. Painter, and J. G. Ferry. 1996. Characterization of an iron-sulfur flavoprotein from Mathanosarina thermophila. J. Biol. Chem. 271: 24023-24028.
17. Mueller, J. G., P. J. Chapman, and P. H. Pritchard. 1989. Creosote-contaminated sites - their potential for bioremediation. Environ. Sci. Technol. 23: 1197-1201.
18. Parales, R. E., J. G. Parales, and D. T. Gibson. 1999. Aspartate 205 in the catalytic domain of naphthalene dioxygenase is essential for activity. J. Bacteriol. 181:1831-1837.
19. Pearson, W. R., and D. J. Lipman. 1988. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA 85:2444-2448.
20. Pikus, J. D., J. M. Studts, C. Adim, K. E. Kauffmann, E. Munck, R. J. Stefan, K. McClay, and B. G. Fox. 1996. Recombinant toluene-4-monooxygenase: catalytic and Mössbauer studies of the purified diiron and Rieske components of a four-protein complex. Biochemistry 35:9106-9119.
21. Shine, J., and L. Dalgarno. 1974. The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosomal binding sites. Proc. Natl. Acad. Sci. USA 71:1342-1346.
22. Siegel, L. M. 1965. A direct microdetermination for sulfide. Anal. Biochem. 11:126-132.
23. Simon, M. J., T. D. Osslund, R. Saunders, B. D. Ensley, S. Suggs, A. Harcourt, W. C. Suen, D. L. Cruden, D. T. Gibson, and G. J. Zylstra. 1993. Sequences of genes encoding naphthalene dioxygenase in Pseudomonas putida strains G7 and NCIB 9816-4. Gene 127:31-37.
24. Suen, W. C., B. E. Haigler, and J. C. Spain. 1996. 2.4-Dinitrotoluene dioxygenase from Burkholderia sp. strain DNT: similarity to naphthalene dioxygenase. J. Bacteriol. 178:4926-4934.
25. Warhurst, A. M., and C. A. Fewson. 1994. Biotransformations catalyzed by the genus Rhodococcus. Crit. Rev. Biotechnol. 14:29-73.