메뉴 건너뛰기




Volumn 71, Issue 9, 2005, Pages 5354-5361

Epoxide formation on the aromatic B ring of flavanone by biphenyl dioxygenase of Pseudomonas pseudoalcaligenes KF707

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC COMPOUNDS; CHEMICAL BONDS; HIGH PRESSURE LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; METABOLITES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

EID: 25144477568     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.71.9.5354-5361.2005     Document Type: Article
Times cited : (21)

References (45)
  • 1
    • 0001516757 scopus 로고
    • A simple method for suppressing dispersion-mode contributions in NMR spectra: The "pseudo echo"
    • Bax, A., and R. Freeman. 1981. A simple method for suppressing dispersion-mode contributions in NMR spectra: the "pseudo echo." J. Magn. Reson. 43:333-338.
    • (1981) J. Magn. Reson. , vol.43 , pp. 333-338
    • Bax, A.1    Freeman, R.2
  • 2
    • 33644757144 scopus 로고
    • Correlation of proton and nitrogen-15 chemical shifts by multiple quantum NMR
    • Bax, A., R. Griffey, and B. Hawkins. 1983. Correlation of proton and nitrogen-15 chemical shifts by multiple quantum NMR. J. Magn. Reson. 55:301-315.
    • (1983) J. Magn. Reson. , vol.55 , pp. 301-315
    • Bax, A.1    Griffey, R.2    Hawkins, B.3
  • 3
    • 0345311216 scopus 로고
    • 13C assignments from sensitivity-enhanced detection of heteronuclear multiple-bond connectivity by 2D multiple quantum NMR
    • 13C assignments from sensitivity-enhanced detection of heteronuclear multiple-bond connectivity by 2D multiple quantum NMR. J. Am. Chem. Soc. 108:2093-2094.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 2093-2094
    • Bax, A.1    Summers, M.2
  • 4
    • 0035711112 scopus 로고    scopus 로고
    • Aromatic dioxygenases: Molecular biocatalysis and applications
    • Boyd, D. R., N. D. Sharma, and C. C. Allen. 2001. Aromatic dioxygenases: molecular biocatalysis and applications. Curr. Opin. Biotechnol. 12:564-573.
    • (2001) Curr. Opin. Biotechnol. , vol.12 , pp. 564-573
    • Boyd, D.R.1    Sharma, N.D.2    Allen, C.C.3
  • 6
    • 0019052887 scopus 로고
    • Fungal oxidation of (+/-)-9,10-dihydroxy-9,10-dihydrobenzo[a]pyrene: Formation of diastereomeric benzo[a]pyrene 9,10-diol 7,8-epoxides
    • Cerniglia, C. E., and D. T. Gibson. 1980. Fungal oxidation of (+/-)-9,10-dihydroxy-9,10-dihydrobenzo[a]pyrene: formation of diastereomeric benzo[a]pyrene 9,10-diol 7,8-epoxides. Proc. Natl. Acad. Sci. USA 77:4554-4558.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 4554-4558
    • Cerniglia, C.E.1    Gibson, D.T.2
  • 7
    • 0018941268 scopus 로고
    • Fungal oxidation of benzo[a]pyrene and (+/-)-trans-7,8-dihydroxy-7,8- dihydrobenzo[a]pyrene. Evidence for the formation of a benzo[a]pyrene 7,8-diol-9,10-epoxide
    • Cerniglia, C. E., and D. T., Gibson. 1980. Fungal oxidation of benzo[a]pyrene and (+/-)-trans-7,8-dihydroxy-7,8-dihydrobenzo[a]pyrene. Evidence for the formation of a benzo[a]pyrene 7,8-diol-9,10-epoxide. J. Biol. Chem. 255:5159-5163.
    • (1980) J. Biol. Chem. , vol.255 , pp. 5159-5163
    • Cerniglia, C.E.1    Gibson, D.T.2
  • 8
    • 0018378931 scopus 로고
    • Bacterial and fungal oxidation of dibenzofuran
    • Cerniglia, C. E., J. C. Morgan, and D. T. Gibson, 1979. Bacterial and fungal oxidation of dibenzofuran. Biochem. J. 180:175-185.
    • (1979) Biochem. J. , vol.180 , pp. 175-185
    • Cerniglia, C.E.1    Morgan, J.C.2    Gibson, D.T.3
  • 9
    • 0037448299 scopus 로고    scopus 로고
    • Biotransformation of flavone and flavanone by Streptomyces lividans cells carrying shuffled biphenyl dioxygenase genes
    • Chun, H. K., Y. Ohnishi, K. Shindo, N. Misawa, K. Furukawa, and S. Horinouchi. 2003. Biotransformation of flavone and flavanone by Streptomyces lividans cells carrying shuffled biphenyl dioxygenase genes. J. Mol. Catal. B Enzymatic 21:113-121.
    • (2003) J. Mol. Catal. B Enzymatic , vol.21 , pp. 113-121
    • Chun, H.K.1    Ohnishi, Y.2    Shindo, K.3    Misawa, N.4    Furukawa, K.5    Horinouchi, S.6
  • 10
    • 0036525713 scopus 로고    scopus 로고
    • Protein engineering of oxygenases for biocatalysis
    • Cirino, P. C., and F. H. Arnold. 2002. Protein engineering of oxygenases for biocatalysis. Curr. Opin. Chem. Biol. 6:130-135.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 130-135
    • Cirino, P.C.1    Arnold, F.H.2
  • 11
    • 1542378704 scopus 로고    scopus 로고
    • Dioxygen activation at mononuclear nonheme iron active sites: Enzymes, models, and intermediates
    • Costas, M., M. P. Mehn, M. P. Jensen, and L. J. Que. 2004. Dioxygen activation at mononuclear nonheme iron active sites: enzymes, models, and intermediates. Chem. Rev. 104:939-986.
    • (2004) Chem. Rev. , vol.104 , pp. 939-986
    • Costas, M.1    Mehn, M.P.2    Jensen, M.P.3    Que, L.J.4
  • 13
    • 0041045434 scopus 로고
    • Distortionless enhancement of NMR signals by polarization transfer
    • Dodrell, D., D. Pegg, and M. Bendall. 1982. Distortionless enhancement of NMR signals by polarization transfer. J. Magn. Reson. 48:323-327.
    • (1982) J. Magn. Reson. , vol.48 , pp. 323-327
    • Dodrell, D.1    Pegg, D.2    Bendall, M.3
  • 14
    • 0020806085 scopus 로고
    • Naphthalene dioxygenase: Purification and properties of a terminal oxygenase component
    • Ensley, B. D., and D. T. Gibson. 1983. Naphthalene dioxygenase: purification and properties of a terminal oxygenase component. J. Bacteriol. 155:505-511.
    • (1983) J. Bacteriol. , vol.155 , pp. 505-511
    • Ensley, B.D.1    Gibson, D.T.2
  • 16
    • 0034082905 scopus 로고    scopus 로고
    • Engineering dioxygenases for efficient degradation of environmental pollutants
    • Furukawa, K. 2000. Engineering dioxygenases for efficient degradation of environmental pollutants. Curr. Opin. Biotechnol. 11:244-249.
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 244-249
    • Furukawa, K.1
  • 17
    • 0023114367 scopus 로고
    • Purification and properties of 2,3-dihydroxybiphenyl dioxygenase from polychlorinated biphenyl-degrading Pseudomonas pseudoalcaligenes and Pseudomonas aeruginosa carrying the cloned bphC gene
    • Furukawa, K., and N. Arimura. 1987. Purification and properties of 2,3-dihydroxybiphenyl dioxygenase from polychlorinated biphenyl-degrading Pseudomonas pseudoalcaligenes and Pseudomonas aeruginosa carrying the cloned bphC gene. J. Bacteriol. 169:924-927.
    • (1987) J. Bacteriol. , vol.169 , pp. 924-927
    • Furukawa, K.1    Arimura, N.2
  • 18
    • 0022617112 scopus 로고
    • Cloning of a gene cluster encoding biphenyl and chlorobiphenyl degradation in Pseudomonas pseudoalcaligenes
    • Furukawa, K., and T. Miyazaki. 1986. Cloning of a gene cluster encoding biphenyl and chlorobiphenyl degradation in Pseudomonas pseudoalcaligenes. J. Bacteriol. 166:392-398.
    • (1986) J. Bacteriol. , vol.166 , pp. 392-398
    • Furukawa, K.1    Miyazaki, T.2
  • 19
    • 49849107557 scopus 로고
    • Circular dichroism, optical rotatory dispersion and absolute configuration of flavanones, 3-hydroxyflavanones and their glycosides: Determination of aglycone chirality in flavanone glycosides
    • Gaffield, W. 1970. Circular dichroism, optical rotatory dispersion and absolute configuration of flavanones, 3-hydroxyflavanones and their glycosides: determination of aglycone chirality in flavanone glycosides. Tetrahedron 26:4093-4108.
    • (1970) Tetrahedron , vol.26 , pp. 4093-4108
    • Gaffield, W.1
  • 20
    • 0027183124 scopus 로고
    • Oxidation of polychlorinated biphenyls by Pseudomonas sp. strain LB400 and Pseudomonas pseudoalcaligenes KF707
    • Gibson, D. T., D. L. Cruden, J. D. Haddock, G. J. Zylstra, and J. M. Brand. 1993. Oxidation of polychlorinated biphenyls by Pseudomonas sp. strain LB400 and Pseudomonas pseudoalcaligenes KF707. J. Bacteriol. 175:4561-4564.
    • (1993) J. Bacteriol. , vol.175 , pp. 4561-4564
    • Gibson, D.T.1    Cruden, D.L.2    Haddock, J.D.3    Zylstra, G.J.4    Brand, J.M.5
  • 21
    • 0037223878 scopus 로고    scopus 로고
    • Cytochrome P450 oxidations in the generation of reactive electrophiles: Epoxidation and related reactions
    • Guengerich, F. P. 2003. Cytochrome P450 oxidations in the generation of reactive electrophiles: epoxidation and related reactions. Arch. Biochem. Biophys. 409:59-71.
    • (2003) Arch. Biochem. Biophys. , vol.409 , pp. 59-71
    • Guengerich, F.P.1
  • 22
    • 0028215858 scopus 로고
    • Construction of hybrid biphenyl (bph) and toluene (tod) genes for functional analysis of aromatic ring dioxygenases
    • Hirose, J., A. Suyama, S. Hayashida, and K. Furukawa. 1994. Construction of hybrid biphenyl (bph) and toluene (tod) genes for functional analysis of aromatic ring dioxygenases. Gene 138:27-33.
    • (1994) Gene , vol.138 , pp. 27-33
    • Hirose, J.1    Suyama, A.2    Hayashida, S.3    Furukawa, K.4
  • 23
    • 0032819772 scopus 로고    scopus 로고
    • Dietary flavonoids: Intake, health effects and bioavailability
    • Hollman, P. C., and M. B. Katan. 1999. Dietary flavonoids: intake, health effects and bioavailability. Food Chem. Toxicol. 37:937-942.
    • (1999) Food Chem. Toxicol. , vol.37 , pp. 937-942
    • Hollman, P.C.1    Katan, M.B.2
  • 24
    • 0033387699 scopus 로고    scopus 로고
    • Health effects and bioavailability of dietary flavonols
    • Hollman, P. C., and M. B. Katan. 1999. Health effects and bioavailability of dietary flavonols. Free Radic. Res. 31(Suppl.):S75-S80.
    • (1999) Free Radic. Res. , vol.31 , Issue.SUPPL.
    • Hollman, P.C.1    Katan, M.B.2
  • 25
    • 0035003513 scopus 로고    scopus 로고
    • Hydroxylations and methylations of quercetin, fisetin, and catechin by Streptomyces griseus
    • Hosny, M., K. Dhar, and J. P. Rosazza. 2001. Hydroxylations and methylations of quercetin, fisetin, and catechin by Streptomyces griseus. J. Nat. Prod. 64:462-465.
    • (2001) J. Nat. Prod. , vol.64 , pp. 462-465
    • Hosny, M.1    Dhar, K.2    Rosazza, J.P.3
  • 26
    • 0025425581 scopus 로고
    • Microbiological transformation of (+/-)-flavanone and (+/-)-isoflavanone
    • Ibrahim, A. R., and Y. J. Abul-Hajj. 1990. Microbiological transformation of (+/-)-flavanone and (+/-)-isoflavanone. J. Nat. Prod. 53:644-656.
    • (1990) J. Nat. Prod. , vol.53 , pp. 644-656
    • Ibrahim, A.R.1    Abul-Hajj, Y.J.2
  • 27
    • 0014974950 scopus 로고
    • cis-1,2-dihydroxy-1,2-dihydronaphthalene: A bacterial metabolite from naphthalene
    • Jerina, D. M., J. W. Daly, A. M. Jeffrey, and D. T. Gibson. 1971. cis-1,2-Dihydroxy-1,2-dihydronaphthalene: a bacterial metabolite from naphthalene. Arch. Biochem. Biophys. 142:394-396.
    • (1971) Arch. Biochem. Biophys. , vol.142 , pp. 394-396
    • Jerina, D.M.1    Daly, J.W.2    Jeffrey, A.M.3    Gibson, D.T.4
  • 28
    • 0014405152 scopus 로고
    • The role of arene oxide-oxepin systems in the metabolism of aromatic substrates. 3. Formation of 1,2-naphthalene oxide from naphthalene by liver microsomes
    • Jerina, D. M., J. W. Daly, B. Witkop, P. Zaltzman-Nirenberg, and S. Udenfriend. 1968. The role of arene oxide-oxepin systems in the metabolism of aromatic substrates. 3. Formation of 1,2-naphthalene oxide from naphthalene by liver microsomes. J. Am. Chem. Soc. 90:6525-6527.
    • (1968) J. Am. Chem. Soc. , vol.90 , pp. 6525-6527
    • Jerina, D.M.1    Daly, J.W.2    Witkop, B.3    Zaltzman-Nirenberg, P.4    Udenfriend, S.5
  • 29
    • 0347264753 scopus 로고    scopus 로고
    • Crystal structure of naphthalene dioxygenase: Side-on binding of dioxygen to iron
    • Karlsson, A., J. V. Parales, R. E. Parales, D. T. Gibson, H. Eklund, and S. Ramaswamy. 2003. Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron. Science 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
    • 2942530416 scopus 로고    scopus 로고
    • Saturation mutagenesis of Burkholderia cepacia R34 2,4-dinitrotoluene dioxygenase at DntAc valine 350 for synthesizing nitrohydroquinone, methylhydroquinone, and methoxyhydroquinone
    • Keenan, B. G., T. Leungsakul, B. F. Smets, and T. K. Wood. 2004. Saturation mutagenesis of Burkholderia cepacia R34 2,4-dinitrotoluene dioxygenase at DntAc valine 350 for synthesizing nitrohydroquinone, methylhydroquinone, and methoxyhydroquinone. Appl. Environ. Microbiol. 70:3222-3231.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 3222-3231
    • Keenan, B.G.1    Leungsakul, T.2    Smets, B.F.3    Wood, T.K.4
  • 32
    • 0242437987 scopus 로고    scopus 로고
    • cis-2′,3′-Dihydrodiol production on flavone B-ring by biphenyl dioxygenase from Pseudomonas pseudoalcaligenes KF707 expressed in Escherichia coli
    • Kim, S.-Y., J. Jung, Y. Lim, J.-H. Ahn, S.-I. Kim, and H.-G. Hur. 2003. cis-2′,3′-Dihydrodiol production on flavone B-ring by biphenyl dioxygenase from Pseudomonas pseudoalcaligenes KF707 expressed in Escherichia coli. Antonie Leeuwenhoek 84:261-268.
    • (2003) Antonie Leeuwenhoek , vol.84 , pp. 261-268
    • Kim, S.-Y.1    Jung, J.2    Lim, Y.3    Ahn, J.-H.4    Kim, S.-I.5    Hur, H.-G.6
  • 33
    • 0037386617 scopus 로고    scopus 로고
    • Insight into the mechanism of aromatic hydroxylation by toluene 4-monooxygenase by use of specifically deuterated toluene and p-xylene
    • Mitchell, K. H., C. E. Rogge, T. Gierahn, and B. G. Fox. 2003. Insight into the mechanism of aromatic hydroxylation by toluene 4-monooxygenase by use of specifically deuterated toluene and p-xylene. Proc. Natl. Acad. Sci. USA 100:3784-3789.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 3784-3789
    • Mitchell, K.H.1    Rogge, C.E.2    Gierahn, T.3    Fox, B.G.4
  • 35
    • 0015426160 scopus 로고
    • A reconstituted microsomal enzyme system that converts naphthalene to trans-1,2-dihydroxy-1,2-dihydroriaphthalene via naphthalene-1,2-oxide: Presence of epoxide hydrase in cytochrome P-450 and P-448 fractions
    • Oesch, F., D. M. Jerina, J. W. Daly, A. Y. Lu, R. Kuntzman, and A. H. Conney. 1972. A reconstituted microsomal enzyme system that converts naphthalene to trans-1,2-dihydroxy-1,2-dihydroriaphthalene via naphthalene-1,2-oxide: presence of epoxide hydrase in cytochrome P-450 and P-448 fractions. Arch. Biochem. Biophys. 153:62-67.
    • (1972) Arch. Biochem. Biophys. , vol.153 , pp. 62-67
    • Oesch, F.1    Jerina, D.M.2    Daly, J.W.3    Lu, A.Y.4    Kuntzman, R.5    Conney, A.H.6
  • 36
    • 0030513196 scopus 로고    scopus 로고
    • Diverse reactions catalyzed by naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816
    • Resnick, S. M., K. Lee, and D. T. Gibson. 1996. Diverse reactions catalyzed by naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816. J. Ind. Microbiol. 17:438-457.
    • (1996) J. Ind. Microbiol. , vol.17 , pp. 438-457
    • Resnick, S.M.1    Lee, K.2    Gibson, D.T.3
  • 38
    • 0016591915 scopus 로고
    • Metabolism of chlorobenzene with hepatic microsomes and solubilized cytochrome P-450 systems
    • Selander, H. G., D. M. Jerina, and J. W. Daly. 1975. Metabolism of chlorobenzene with hepatic microsomes and solubilized cytochrome P-450 systems. Arch. Biochem. Biophys. 168:309-321.
    • (1975) Arch. Biochem. Biophys. , vol.168 , pp. 309-321
    • Selander, H.G.1    Jerina, D.M.2    Daly, J.W.3
  • 39
    • 0024025210 scopus 로고
    • Oxidation of substituted phenols by Pseudomonas putida F1 and Pseudomonas sp. strain JS6
    • Spain, J. C., and D. T. Gibson. 1988. Oxidation of substituted phenols by Pseudomonas putida F1 and Pseudomonas sp. strain JS6. Appl. Environ. Microbiol. 54:1399-1404.
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 1399-1404
    • Spain, J.C.1    Gibson, D.T.2
  • 40
    • 0021895134 scopus 로고
    • Purification and properties of ferredoxinTOL. A component of toluene dioxygenase from Pseudomonas putida F1
    • Subramanian, V., T. N. Liu, W. K. Yeh, C. M. Serdar, L. P. Wackett, and D. T. Gibson. 1985. Purification and properties of ferredoxinTOL. A component of toluene dioxygenase from Pseudomonas putida F1. J. Biol. Chem. 260:2355-2363.
    • (1985) J. Biol. Chem. , vol.260 , pp. 2355-2363
    • Subramanian, V.1    Liu, T.N.2    Yeh, W.K.3    Serdar, C.M.4    Wackett, L.P.5    Gibson, D.T.6
  • 41
    • 0034878844 scopus 로고    scopus 로고
    • Directed evolution of biphenyl dioxygenase: Emergence of enhanced degradation capacity for benzene, toluene, and alkylbenzenes
    • Suenaga, H., M. Mitsuoka, Y. Ura, T. Watanabe, and K. Furukawa. 2001. Directed evolution of biphenyl dioxygenase: emergence of enhanced degradation capacity for benzene, toluene, and alkylbenzenes. J. Bacteriol. 183:5441-5444.
    • (2001) J. Bacteriol. , vol.183 , pp. 5441-5444
    • Suenaga, H.1    Mitsuoka, M.2    Ura, Y.3    Watanabe, T.4    Furukawa, K.5
  • 42
    • 3242763195 scopus 로고    scopus 로고
    • Oxidation of benzene to phenol, catechol, and 1,2,3-trihyroxybenzene by toluene 4-monooxygenase of Pseudomonas mendocina KR1 and toluene 3-monooxygenase of Ralstonia pickettii PK01
    • Tao, Y., A. Fishman, W. E. Bentley, and T. K. Wood. 2004. Oxidation of benzene to phenol, catechol, and 1,2,3-trihyroxybenzene by toluene 4-monooxygenase of Pseudomonas mendocina KR1 and toluene 3-monooxygenase of Ralstonia pickettii PK01. Appl. Environ. Microbiol. 70:3814-3820.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 3814-3820
    • Tao, Y.1    Fishman, A.2    Bentley, W.E.3    Wood, T.K.4
  • 43
    • 2942592050 scopus 로고    scopus 로고
    • Protein engineering of toluene-o-xylene monooxygenase from Pseudomonas stutzen OX1 for synthesizing 4-methylresorcinol, methylhydroquinone, and pyrogallol
    • Vardar, G., and T. K. Wood. 2004. Protein engineering of toluene-o-xylene monooxygenase from Pseudomonas stutzen OX1 for synthesizing 4-methylresorcinol, methylhydroquinone, and pyrogallol. Appl. Environ. Microbiol. 70:3253-3262.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 3253-3262
    • Vardar, G.1    Wood, T.K.2
  • 45
    • 0022637899 scopus 로고
    • Identification of cis-diols as intermediates in the oxidation of aromatic acids by a strain of Pseudomonas putida that contains a TOL plasmid
    • Whited, G. M., W. R. McCombie, L. D. Kwart, and D. T. Gibson. 1986. Identification of cis-diols as intermediates in the oxidation of aromatic acids by a strain of Pseudomonas putida that contains a TOL plasmid. J. Bacteriol. 166:1028-1039.
    • (1986) J. Bacteriol. , vol.166 , pp. 1028-1039
    • Whited, G.M.1    McCombie, W.R.2    Kwart, L.D.3    Gibson, D.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.