Both FMNH2 and FADH2 can be utilized by the dibenzothiophene monooxygenase from a desulfurizing bacterium Mycobacterium goodii X7B

Bioresource Technology

Volumn 100, Issue 9, 2009, Pages 2594-2599

  Li, Jingchen ^a   Feng, Jinhui ^a   Li, Qian ^a   Ma, Cuiqing ^a   Yu, Bo ^b   Gao, Chao ^a   Wu, Geng ^c   Xu, Ping ^a,c  

^a SHANDONG UNIVERSITY   (China)

^b INSTITUTE OF MICROBIOLOGY   (China)

^c BEIJING UNIVERSITY OF POSTS AND TELECOMMUNICATIONS   (China)

Author keywords

Biodesulfurization; Dibenzothiophene monooxygenase; FADH2; FMNH2; Mycobacterium goodii

Indexed keywords

BIODESULFURIZATION; DIBENZOTHIOPHENE MONOOXYGENASE; FADH2; FMNH2; MYCOBACTERIUM GOODII;

COENZYMES; ENZYME ACTIVITY; ESCHERICHIA COLI;

DESULFURIZATION;

DIBENZOTHIOPHENE DERIVATIVE; FLAVOPROTEIN; 1,5 DIHYDRO FAD; 1,5-DIHYDRO-FAD; BACTERIAL PROTEIN; DIBENZOTHIOPHENE MONOOXYGENASE; DRUG DERIVATIVE; FLAVINE ADENINE NUCLEOTIDE; FLAVINE MONONUCLEOTIDE; OXIDOREDUCTASE;

BACTERIUM; CATALYSIS; ENZYME ACTIVITY; OXIDATION; RECOMBINATION; SUBSTRATE;

ACINETOBACTER BAUMANNII; ARTICLE; BACTERIAL STRAIN; DESULFURIZATION; ESCHERICHIA COLI; MYCOBACTERIUM; MYCOBACTERIUM GOODII; NONHUMAN; NUCLEOTIDE SEQUENCE; OXIDATION; PRIORITY JOURNAL; SEQUENCE ANALYSIS; AMINO ACID SEQUENCE; BIOCATALYSIS; BIOREMEDIATION; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; OXIDATION REDUCTION REACTION; PHYLOGENY; SEQUENCE ALIGNMENT;

ACINETOBACTER BAUMANNII; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; MYCOBACTERIUM GOODII;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BIOCATALYSIS; BIODEGRADATION, ENVIRONMENTAL; CLONING, MOLECULAR; ESCHERICHIA COLI; FLAVIN MONONUCLEOTIDE; FLAVIN-ADENINE DINUCLEOTIDE; MOLECULAR SEQUENCE DATA; MYCOBACTERIUM; OXIDATION-REDUCTION; OXIDOREDUCTASES; PHYLOGENY; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, PROTEIN; SUBSTRATE SPECIFICITY;

EID: 59649083929     PISSN: 09608524     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biortech.2008.12.009     Document Type: Article

References (35)

1. Alfieri A., Fersini F., Ruangchan N., Prongjit M., Chaiyen P., and Mattevi A. Structure of the monooxygenase component of a two-component flavoprotein monooxygenase. Proc. Natl. Acad. Sci. USA 104 (2007) 1177-1182
2. Chaiyen P., Suadee C., and Wilairat P.A. A novel two-protein component flavoprotein hydroxylase p-hydroxyphenylacetate hydroxylase from Acinetobacter baumannii. Eur. J. Biochem. 268 (2001) 5550-5561
3. Chen H., Zhang W., Cai Y., Zhang Y., and Li W. Elucidation of 2-hydroxybiphenyl effect on dibenzothiophene desulfurization by Microbacterium sp. strain ZD-M2. Bioresour. Technol. 99 (2008) 6928-6933
4. Cuff J.A., Clamp M.E., Siddiqui A.S., Finlay M., and Barton G.J. Jpred: a consensus secondary structure prediction server. Bioinformatics 14 (1998) 892-893
5. Denome S.A., Oldfield C., Nash L.J., and Young K.D. Characterization of the desulfurization genes from Rhodococcus sp. strain IGTS8. J. Bacteriol. 176 (1994) 6706-6716
6. Duffner F.M., Kirchner U., Bauer M.P., and Muller R. Phenol/cresol degradation by the thermophilic Bacillus thermoglucosidasius A7: cloning and sequence analysis of five genes involved in the pathway. Gene 256 (2000) 215-221
7. Eichhorn E., van der Ploeg J.R., and Leisinger T. Characterization of a two-component alkanesulfonate monooxygenase from Escherichia coli. J. Biol. Chem. 274 (1999) 26639-26646
8. Furuya T., Takahashi S., Iwasaki Y., Ishii Y., Kino K., and Kirimura K. Gene cloning and characterization of Mycobacterium phlei flavin reductase involved in dibenzothiophene desulfurization. J. Biosci. Bioeng. 99 (2005) 577-585
9. Galán B., Díaz E., and García J.L. Enhancing desulphurization by engineering a flavin reductase-encoding gene cassette in recombinant biocatalysts. Environ. Microbiol. 2 (2000) 687-694
10. Gibson Q.H., and Hastings J.W. The oxidation of reduced flavin mononucleotide by molecular oxygen. Biochem. J. 83 (1962) 368-377
11. Gray K.A., Pogrebinsky O.S., Mrachko G.T., Xi L., Monticello D.J., and Squires C.H. Molecular mechanism of biocatalytic desulfurization of fossil fuels. Nat. Biotechnol. 14 (1996) 1705-1709
12. Joosten V., and van Berkel W.J.H. Flavoenzymes. Curr. Opin. Chem. Biol. 11 (2007) 195-202
13. Kahnert A., Vermeij P., Wietek C., James P., Leisinger T., and Kerteszi M.A. The ssu locus plays a key role in organosulfur metabolism in Pseudomonas putida S-313. J. Bacteriol. 182 (2000) 2869-2878
14. Kertesz M.A., and Wietek C. Desulfurization and desulfonation: applications of sulfur-controlled gene expression in bacteria. Appl. Microbiol. Biotechnol. 57 (2001) 460-466
15. Kim S., Hisano T., Takeda K., Iwasaki W., Ebihara A., and Miki K. Crystal structure of the oxygenase component (HpaB) of the 4-hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8. J. Biol. Chem. 282 (2007) 33107-33116
16. Knobel H.R., Egli T., and van der Meer J.R. Cloning and characterization of the genes encoding nitrilotriacetate monooxygenase of Chelatobacter heintzii ATCC 29600. J. Bacteriol. 178 (1996) 6123-6132
17. Lei B., and Tu S. Mechanism of reduced flavin transfer from Vibrio harveyi NADPH-FMN oxidoreductase to luciferase. Biochemistry 37 (1998) 14623-14629
18. Li F.L., Xu P., Feng J.H., Meng L., Zheng Y., Luo L.L., and Ma C.Q. Microbial desulfurization of gasoline in a Mycobacterium goodii X7B immobilized-cell system. Appl. Environ. Microbiol. 71 (2005) 276-281
19. Li F.L., Xu P., Ma C.Q., Luo L.L., and Wang X.S. Deep desulfurization of hydrodesulfurization-treated diesel oil by a facultative thermophilic bacterium Mycobacterium sp. X7B. FEMS. Microbiol. Lett. 223 (2003) 301-307
20. Louie T.M., Webster C.M., and Xun L. Genetic and biochemical characterization of a 2,4,6-trichlorophenol degradation pathway in Ralstonia eutropha JMP134. J. Bacteriol. 184 (2002) 3492-3500
21. Louie T.M., Yang H., Karnchanaphanurach P., Xie X.S., and Xun L. FAD is a preferred substrate and an inhibitor of Escherichia coli general NAD(P)H: flavin oxidoreductase. J. Biol. Chem. 277 (2002) 39450-39455
22. Ohshiro T., Suzuki K., and Izumi Y. Dibenzothiophene (DBT) degrading enzyme responsible for the first step of DBT desulfurization by Rhodococcus erythropolis D-l: purification and characterization. J. Ferm. Bioeng. 83 (1997) 233-237
23. Ohshiro T., Yamada H., Shimoda T., Matsubara T., and Izumi Y. Thermostable flavin reductase that couples with dibenzothiophene monooxygenase, from thermophilic Bacillus sp. DSM411: purification, characterization, and gene cloning. Biosci. Biotechnol. Biochem. 68 (2004) 1712-1721
24. Parry R.J., and Li W. Purification and characterization of isobutylamine N-hydroxylase from the valanimycin producer Streptomyces viridifaciens Mg456-hF10. Arch. Biochem. Biophys. 339 (1997) 47-54
25. Payne J.W., Bolton Jr. H., Campbell J.A., and Xun L. Purification and characterization of EDTA monooxygenase from the EDTA-degrading bacterium BNC1. J. Bacteriol. 180 (1998) 3823-3827
26. Prieto M.A., and Garcia J.L. Molecular characterization of 4-hydroxyphenylacetate 3-hydroxylase of Escherichia coli. A two-protein component enzyme. J. Biol. Chem. 269 (1994) 22823-22829
27. Reichmuth D.S., Hittle J.L., Blanch H.W., and Keasling J.D. Biodesulfurization of dibenzothiophene in Escherichia coli is enhanced by expression of Vibrio harveyi oxidoreductase gene. Biotechnol. Bioeng. 67 (2000) 72-79
28. Seki M., Iida K., Saito M., Nakayama H., and Yoshida S. Hydrogen peroxide production in Streptococcus pyogenes: involvement of lactate oxidase and coupling with aerobic utilization of lactate. J. Bacteriol. 186 (2004) 2046-2051
29. Shavandi M., Sadeghizadeh M., Zomorodipour A., and Khajeh K. Biodesulfurization of dibenzothiophene by recombinant Gordonia alkanivorans RIPI90A. Bioresour. Technol. 100 (2009) 475-479
30. Sucharitakul J., Chaiyen P., Entsch B., and Ballou D.P. Kinetic mechanisms of the oxygenase from a two-component enzyme, p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii. J. Biol. Chem. 281 (2006) 17044-17053
31. Tamura K., Dudley J., Nei M., and Kumar S. MEGA 4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24 (2007) 1596-1599
32. Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., and Higgins D.G. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 24 (1997) 4876-4882
33. Thotsaporn K., Sucharitakul J., Wongratana J., Suadee C., and Chaiyen P. 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 (2004) 60-66
34. van Berkel W.J.H., Kamerbeek N.M., and Fraaije M.W. Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts. J. Biotechnol. 124 (2006) 670-689
35. Zdobnov E.M., and Apweiler R. InterProScan - an integration platform for the signature-recognition methods in InterPro. Bioinformatics 17 (2001) 847-848