메뉴 건너뛰기




Volumn 421, Issue 4, 2012, Pages 757-762

Structural insights into the metabolism of 2-chlorodibenzofuran by an evolved biphenyl dioxygenase

Author keywords

Biocatalysis; Burkholderia xenovorans LB400; Chlorodibenzofurans; Directed evolution; Enzyme engineering; Rieske type oxygenase

Indexed keywords

2 CHLORODIBENZOFURAN; BIPHENYL DIOXYGENASE; DIBENZOFURAN DERIVATIVE; DIOXYGENASE; OXYGEN; UNCLASSIFIED DRUG;

EID: 84861223438     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.04.078     Document Type: Article
Times cited : (20)

References (33)
  • 1
    • 84861225639 scopus 로고    scopus 로고
    • Engineering microbial enzymes and plants to promote PCB degradation in soil: Current state of knowledge
    • Caister Academic Press, Norfolk, U.K. A.I. Koukkou (Ed.)
    • Sylvestre M., Toussaint J.P. Engineering microbial enzymes and plants to promote PCB degradation in soil: Current state of knowledge. Microbial Bioremediation of Non-metals Current Research 2011, 177-196. Caister Academic Press, Norfolk, U.K. A.I. Koukkou (Ed.).
    • (2011) Microbial Bioremediation of Non-metals Current Research , pp. 177-196
    • Sylvestre, M.1    Toussaint, J.P.2
  • 2
    • 22544474316 scopus 로고    scopus 로고
    • Resolving the profile of metabolites generated during oxidation of dibenzofuran and chlorodibenzofurans by the biphenyl catabolic pathway enzymes
    • Mohammadi M., Sylvestre M. Resolving the profile of metabolites generated during oxidation of dibenzofuran and chlorodibenzofurans by the biphenyl catabolic pathway enzymes. Chem. Biol. 2005, 12:835-846.
    • (2005) Chem. Biol. , vol.12 , pp. 835-846
    • Mohammadi, M.1    Sylvestre, M.2
  • 3
    • 33645677539 scopus 로고    scopus 로고
    • Arene cis-dihydrodiol formation: From biology to application
    • Boyd D.R., Bugg T.D.H. Arene cis-dihydrodiol formation: From biology to application. Org. Biomol. Chem. 2006, 4:181-192.
    • (2006) Org. Biomol. Chem. , vol.4 , pp. 181-192
    • Boyd, D.R.1    Bugg, T.D.H.2
  • 4
    • 0037448299 scopus 로고    scopus 로고
    • Biotransformation of flavone and flavanone by Streptomyces lividans cells carrying shuffled biphenyl dioxygenase genes
    • Chun H.K., Ohnishi Y., Shindo K., Misawa N., Furukawa K., Horinouchi S. Biotransformation of flavone and flavanone by Streptomyces lividans cells carrying shuffled biphenyl dioxygenase genes. J. Mol. Catal. B: Enzym. 2003, 21:113-121.
    • (2003) J. Mol. Catal. B: Enzym. , vol.21 , pp. 113-121
    • Chun, H.K.1    Ohnishi, Y.2    Shindo, K.3    Misawa, N.4    Furukawa, K.5    Horinouchi, S.6
  • 5
    • 51549085431 scopus 로고    scopus 로고
    • Protein engineering on biphenyl dioxygenase for conferring activity to convert 7-hydroxyflavone and 5,7-dihydroxyflavone (chrysin)
    • Kagami O., Shindo K., Kyojima A., Takeda K., Ikenaga H., Furukawa K., Misawa N. Protein engineering on biphenyl dioxygenase for conferring activity to convert 7-hydroxyflavone and 5,7-dihydroxyflavone (chrysin). J. Biosci. Bioeng. 2008, 106:121-127.
    • (2008) J. Biosci. Bioeng. , vol.106 , pp. 121-127
    • Kagami, O.1    Shindo, K.2    Kyojima, A.3    Takeda, K.4    Ikenaga, H.5    Furukawa, K.6    Misawa, N.7
  • 6
    • 9644287784 scopus 로고    scopus 로고
    • Synthesis of vicinal diols from various arenes with a heterocyclic, amino or carboxyl group by using recombinant Escherichia coli cells expressing evolved biphenyl dioxygenase and dihydrodiol dehydrogenase genes
    • Misawa N., Nakamura R., Kagiyama Y., Ikenaga H., Furukawa K., Shindo K. Synthesis of vicinal diols from various arenes with a heterocyclic, amino or carboxyl group by using recombinant Escherichia coli cells expressing evolved biphenyl dioxygenase and dihydrodiol dehydrogenase genes. Tetrahedron 2005, 61:195-204.
    • (2005) Tetrahedron , vol.61 , pp. 195-204
    • Misawa, N.1    Nakamura, R.2    Kagiyama, Y.3    Ikenaga, H.4    Furukawa, K.5    Shindo, K.6
  • 7
    • 84861130197 scopus 로고    scopus 로고
    • Remarkable abilities of Pandoraea pnomenusa B356 biphenyl dioxygenase to metabolize simple flavonoids
    • Pham T.T., Tu Y., Sylvestre M. Remarkable abilities of Pandoraea pnomenusa B356 biphenyl dioxygenase to metabolize simple flavonoids. Appl. Environ. Microbiol. 2012, 78:3560-3570.
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 3560-3570
    • Pham, T.T.1    Tu, Y.2    Sylvestre, M.3
  • 9
    • 27644543882 scopus 로고    scopus 로고
    • Biocatalytic synthesis of monocyclic arene-dihydrodiols and -diols by Escherichia coli cells expressing hybrid toluene/biphenyl dioxygenase and dihydrodiol dehydrogenase genes
    • Shindo K., Nakamura R., Osawa A., Kagami O., Kanoh K., Furukawa K., Misawa N. Biocatalytic synthesis of monocyclic arene-dihydrodiols and -diols by Escherichia coli cells expressing hybrid toluene/biphenyl dioxygenase and dihydrodiol dehydrogenase genes. J. Mol. Catal. B: Enzym. 2005, 35:134-141.
    • (2005) J. Mol. Catal. B: Enzym. , vol.35 , pp. 134-141
    • Shindo, K.1    Nakamura, R.2    Osawa, A.3    Kagami, O.4    Kanoh, K.5    Furukawa, K.6    Misawa, N.7
  • 10
    • 0001846314 scopus 로고    scopus 로고
    • Enzymatic dihydroxylation of aromatics in enantioselective synthesis: Expanding asymmetric methodology
    • Hudlicky T., Gonzalez D., Gibson D.T. Enzymatic dihydroxylation of aromatics in enantioselective synthesis: Expanding asymmetric methodology. Aldrichimica Acta 1999, 32:35-62.
    • (1999) Aldrichimica Acta , vol.32 , pp. 35-62
    • Hudlicky, T.1    Gonzalez, D.2    Gibson, D.T.3
  • 11
    • 0028820268 scopus 로고
    • Purification and characterization of the oxygenase component of biphenyl 2,3-dioxygenase from Pseudomonas sp. strain LB400
    • Haddock J.D., Gibson D.T. Purification and characterization of the oxygenase component of biphenyl 2,3-dioxygenase from Pseudomonas sp. strain LB400. J. Bacteriol. 1995, 177:5834-5839.
    • (1995) J. Bacteriol. , vol.177 , pp. 5834-5839
    • Haddock, J.D.1    Gibson, D.T.2
  • 12
    • 0028865344 scopus 로고
    • Purification and characterization of the Comamonas testosteroni B-356 biphenyl dioxygenase components
    • Hurtubise Y., Barriault D., Powlowski J., Sylvestre M. Purification and characterization of the Comamonas testosteroni B-356 biphenyl dioxygenase components. J. Bacteriol. 1995, 177:6610-6618.
    • (1995) J. Bacteriol. , vol.177 , pp. 6610-6618
    • Hurtubise, Y.1    Barriault, D.2    Powlowski, J.3    Sylvestre, M.4
  • 13
    • 0029877462 scopus 로고    scopus 로고
    • Characterization of active recombinant his-tagged oxygenase component of Comamonas testosteroni B-356 biphenyl dioxygenase
    • Hurtubise Y., Barriault D., Sylvestre M. Characterization of active recombinant his-tagged oxygenase component of Comamonas testosteroni B-356 biphenyl dioxygenase. J. Biol. Chem. 1996, 271:8152-8156.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8152-8156
    • Hurtubise, Y.1    Barriault, D.2    Sylvestre, M.3
  • 15
    • 9144261771 scopus 로고    scopus 로고
    • Evolution of the biphenyl dioxygenase BphA from Burkholderia xenovorans LB400 by random mutagenesis of multiple sites in region III
    • Barriault D., Sylvestre M. Evolution of the biphenyl dioxygenase BphA from Burkholderia xenovorans LB400 by random mutagenesis of multiple sites in region III. J. Biol. Chem. 2004, 279:47480-47488.
    • (2004) J. Biol. Chem. , vol.279 , pp. 47480-47488
    • Barriault, D.1    Sylvestre, M.2
  • 16
    • 84857992459 scopus 로고    scopus 로고
    • Metabolism of chlorobiphenyls by a variant biphenyl dioxygenase exhibiting enhanced activity toward dibenzofuran
    • Viger J.F., Mohammadi M., Barriault D., Sylvestre M. Metabolism of chlorobiphenyls by a variant biphenyl dioxygenase exhibiting enhanced activity toward dibenzofuran. Biochem. Biophys. Res. Commun. 2012, 419:362-367.
    • (2012) Biochem. Biophys. Res. Commun. , vol.419 , pp. 362-367
    • Viger, J.F.1    Mohammadi, M.2    Barriault, D.3    Sylvestre, M.4
  • 17
    • 0030744612 scopus 로고    scopus 로고
    • Identification and characterization of genes encoding carbazole 1,9a-dioxygenase in Pseudomonas sp. strain CA10
    • Sato S.I., Nam J.W., Kasuga K., Nojiri H., Yamane H., Omori T. Identification and characterization of genes encoding carbazole 1,9a-dioxygenase in Pseudomonas sp. strain CA10. J Bacteriol. 1997, 179:4850-4858.
    • (1997) J Bacteriol. , vol.179 , pp. 4850-4858
    • Sato, S.I.1    Nam, J.W.2    Kasuga, K.3    Nojiri, H.4    Yamane, H.5    Omori, T.6
  • 19
    • 78650862965 scopus 로고    scopus 로고
    • Anaerobic crystallization and initial X-ray diffraction data of biphenyl 2,3-dioxygenase from Burkholderia xenovorans LB400: Addition of agarose improved the quality of the crystals
    • Kumar P., Gomez-Gil L., Mohammadi M., Sylvestre M., Eltis L.D., Bolin J.T. Anaerobic crystallization and initial X-ray diffraction data of biphenyl 2,3-dioxygenase from Burkholderia xenovorans LB400: Addition of agarose improved the quality of the crystals. Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. 2011, 67:59-62.
    • (2011) Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. , vol.67 , pp. 59-62
    • Kumar, P.1    Gomez-Gil, L.2    Mohammadi, M.3    Sylvestre, M.4    Eltis, L.D.5    Bolin, J.T.6
  • 20
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 1997, 276:307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 21
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin A., Teplyakov A. MOLREP: An automated program for molecular replacement. J. Appl. Crystallogr. 1997, 30:1022-1025.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 22
    • 0028103275 scopus 로고
    • Collaborative, Computational, and Project, The CCP4 suite: programs for protein crystallography, Acta Crystallogr
    • Collaborative, Computational, and Project, The CCP4 suite: programs for protein crystallography, Acta Crystallogr.,Sec. D: Biol. Crystallogr. 50 (1994) 760-3.
    • (1994) Sec. D: Biol. Crystallogr. , vol.50 , pp. 760-3
  • 25
    • 33845229149 scopus 로고    scopus 로고
    • Electron transfer complex formation between oxygenase and ferredoxin components in Rieske nonheme iron oxygenase system
    • Ashikawa Y., Fujimoto Z., Noguchi H., Habe H., Omori T., Yamane H., Nojiri H. Electron transfer complex formation between oxygenase and ferredoxin components in Rieske nonheme iron oxygenase system. Structure 2006, 14:1779-1789.
    • (2006) Structure , vol.14 , pp. 1779-1789
    • Ashikawa, Y.1    Fujimoto, Z.2    Noguchi, H.3    Habe, H.4    Omori, T.5    Yamane, H.6    Nojiri, H.7
  • 26
    • 33747818007 scopus 로고    scopus 로고
    • CASTp: Computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
    • Dundas J., Ouyang Z., Tseng J., Binkowski A., Turpaz Y., Liang J. CASTp: Computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues. Nucleic Acids Res. 2006, 34:W116-W118.
    • (2006) Nucleic Acids Res. , vol.34
    • Dundas, J.1    Ouyang, Z.2    Tseng, J.3    Binkowski, A.4    Turpaz, Y.5    Liang, J.6
  • 28
    • 0347264753 scopus 로고    scopus 로고
    • Crystal structure of naphthalene dioxygenase: Side-on binding of dioxygen to iron
    • Karlsson A., Parales J.V., Parales R.E., Gibson D.T., Eklund H., Ramaswamy S. Crystal structure of naphthalene dioxygenase: Side-on binding of dioxygen to iron. Science 2003, 299:1039-1042.
    • (2003) Science , vol.299 , pp. 1039-1042
    • Karlsson, A.1    Parales, J.V.2    Parales, R.E.3    Gibson, D.T.4    Eklund, H.5    Ramaswamy, S.6
  • 30
  • 31
    • 0032989253 scopus 로고    scopus 로고
    • Aspartate 205 in the catalytic domain of naphthalene dioxygenase is essential for activity
    • Parales R.E., Parales J.V., Gibson D.T. Aspartate 205 in the catalytic domain of naphthalene dioxygenase is essential for activity. J. Bacteriol. 1999, 181:1831-1837.
    • (1999) J. Bacteriol. , vol.181 , pp. 1831-1837
    • Parales, R.E.1    Parales, J.V.2    Gibson, D.T.3
  • 32
    • 68949212842 scopus 로고    scopus 로고
    • Specific interactions between the ferredoxin and terminal oxygenase components of a class IIB Rieske nonheme iron oxygenase, carbazole 1,9a-dioxygenase
    • Inoue K., Ashikawa Y., Umeda T., Abo M., Katsuki J., Usami Y., Noguchi H., Fujimoto Z., Terada T., Yamane H., Nojiri H. Specific interactions between the ferredoxin and terminal oxygenase components of a class IIB Rieske nonheme iron oxygenase, carbazole 1,9a-dioxygenase. J. Mol. Biol. 2009, 392:436-451.
    • (2009) J. Mol. Biol. , vol.392 , pp. 436-451
    • Inoue, K.1    Ashikawa, Y.2    Umeda, T.3    Abo, M.4    Katsuki, J.5    Usami, Y.6    Noguchi, H.7    Fujimoto, Z.8    Terada, T.9    Yamane, H.10    Nojiri, H.11
  • 33
    • 18944405592 scopus 로고    scopus 로고
    • 2-Oxoquinoline 8-monooxygenase oxygenase component: Active site modulation by Rieske-[2Fe-2S] center oxidation/reduction
    • Martins B.M., Svetlitchnaia T., Dobbek H. 2-Oxoquinoline 8-monooxygenase oxygenase component: Active site modulation by Rieske-[2Fe-2S] center oxidation/reduction. Structure 2005, 13:817-824.
    • (2005) Structure , vol.13 , pp. 817-824
    • Martins, B.M.1    Svetlitchnaia, T.2    Dobbek, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.