메뉴 건너뛰기




Volumn 1, Issue 2, 2010, Pages

Substrate specificity and structural characteristics of the novel Rieske nonheme iron aromatic ring-hydroxylating oxygenases NidAB and NidA3B3 from Mycobacterium vanbaalenii PYR-1

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; RING HYDROXYLATING OXYGENASE NIDA3B3; RING HYDROXYLATING OXYGENASE NIDAB; UNCLASSIFIED DRUG;

EID: 79952141107     PISSN: None     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00135-10     Document Type: Article
Times cited : (69)

References (53)
  • 1
    • 33847168352 scopus 로고
    • Biodegradation of polycyclic aromatic hydrocarbons
    • Cerniglia, C. E. 1992. Biodegradation of polycyclic aromatic hydrocarbons. Biodegradation 3:351-368.
    • (1992) Biodegradation , vol.3 , pp. 351-368
    • Cerniglia, C.E.1
  • 2
    • 0024023560 scopus 로고
    • Mineralization of polycyclic aromatic hydrocarbons by a bacterium isolated from sediment below an oil field
    • Heitkamp, M. A., and C. E. Cerniglia. 1988. Mineralization of polycyclic aromatic hydrocarbons by a bacterium isolated from sediment below an oil field. Appl. Environ. Microbiol. 54:1612-1614.
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 1612-1614
    • Heitkamp, M.A.1    Cerniglia, C.E.2
  • 3
    • 0036866607 scopus 로고    scopus 로고
    • Classification of a polycyclic aromatic hydrocarbon-metabolizing bacterium, Mycobacterium sp. strain PYR-1, as Mycobacterium vanbaalenii sp. nov
    • Khan, A. A., S. J. Kim, D. D. Paine, and C. E. Cerniglia. 2002. Classification of a polycyclic aromatic hydrocarbon-metabolizing bacterium, Mycobacterium sp. strain PYR-1, as Mycobacterium vanbaalenii sp. nov. Int. J. Syst. Evol. Microbiol. 52:1997-2002.
    • (2002) Int. J. Syst. Evol. Microbiol. , vol.52 , pp. 1997-2002
    • Khan, A.A.1    Kim, S.J.2    Paine, D.D.3    Cerniglia, C.E.4
  • 4
    • 26244435811 scopus 로고    scopus 로고
    • Numerical and genetic analysis of polycyclic aromatic hydrocarbon-degrading mycobacteria
    • Kim, Y. H., K. H. Engesser, and C. E. Cerniglia. 2005. Numerical and genetic analysis of polycyclic aromatic hydrocarbon-degrading mycobacteria. Microb. Ecol. 50:110-119.
    • (2005) Microb. Ecol. , vol.50 , pp. 110-119
    • Kim, Y.H.1    Engesser, K.H.2    Cerniglia, C.E.3
  • 5
    • 52749092752 scopus 로고    scopus 로고
    • Recent advances in the biodegradation of polycyclic aromatic hydrocarbons by Mycobacterium species
    • In V. Šašek, J. A. Glaser, and P. Baveye (ed.), Kluwer Academic Publishers, Dordrecht, Netherlands
    • Cerniglia, C. E. 2003. Recent advances in the biodegradation of polycyclic aromatic hydrocarbons by Mycobacterium species, p. 51-73. In V. Šašek, J. A. Glaser, and P. Baveye (ed.), The utilization of bioremediation to reduce soil contamination: problems and solutions. Kluwer Academic Publishers, Dordrecht, Netherlands.
    • (2003) The utilization of bioremediation to reduce soil contamination: Problems and solutions , pp. 51-73
    • Cerniglia, C.E.1
  • 6
    • 0038493555 scopus 로고    scopus 로고
    • Regioand stereoselective metabolism of 7,12-dimethylbenz[a]anthracene by Mycobacterium vanbaalenii PYR-1
    • Moody, J. D., P. P. Fu, J. P. Freeman, and C. E. Cerniglia. 2003. Regioand stereoselective metabolism of 7,12-dimethylbenz[a]anthracene by Mycobacterium vanbaalenii PYR-1. Appl. Environ. Microbiol. 69: 3924-3931.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 3924-3931
    • Moody, J.D.1    Fu, P.P.2    Freeman, J.P.3    Cerniglia, C.E.4
  • 8
    • 16844377208 scopus 로고    scopus 로고
    • Degradation of benz[a]anthracene by Mycobacterium vanbaalenii strain PYR-1
    • Moody, J. D., J. P. Freeman, and C. E. Cerniglia. 2005. Degradation of benz[a]anthracene by Mycobacterium vanbaalenii strain PYR-1. Biodegradation 16:513-526.
    • (2005) Biodegradation , vol.16 , pp. 513-526
    • Moody, J.D.1    Freeman, J.P.2    Cerniglia, C.E.3
  • 9
    • 79952148632 scopus 로고    scopus 로고
    • Degradation of polycyclic aromatic hydrocarbons by Mycobacterium strains
    • In K. N. Timmis (ed.), Springer, Berlin, Germany
    • Kim, S. J., O. Kweon, and C. E. Cerniglia. 2010. Degradation of polycyclic aromatic hydrocarbons by Mycobacterium strains, p. 1865-1880. In K. N. Timmis (ed.), Handbook of hydrocarbon and lipid microbiology. Springer, Berlin, Germany.
    • (2010) Handbook of hydrocarbon and lipid microbiology , pp. 1865-1880
    • Kim, S.J.1    Kweon, O.2    Cerniglia, C.E.3
  • 10
    • 79952182860 scopus 로고    scopus 로고
    • Genomic view of mycobacterial high molecular weight polycyclic aromatic hydrocarbon degradation
    • In K. N. Timmis (ed.), Springer, Berlin, Germany
    • Kweon, O., S. J. Kim, and C. E. Cerniglia. 2010. Genomic view of mycobacterial high molecular weight polycyclic aromatic hydrocarbon degradation, p. 1165-1178. In K. N. Timmis (ed.), Handbook of hydrocarbon and lipid microbiology. Springer, Berlin, Germany.
    • (2010) Handbook of hydrocarbon and lipid microbiology , pp. 1165-1178
    • Kweon, O.1    Kim, S.J.2    Cerniglia, C.E.3
  • 11
    • 33144467842 scopus 로고    scopus 로고
    • Molecular cloning and expression of genes encoding a novel dioxygenase involved in lowand high-molecular-weight polycyclic aromatic hydrocarbon degradation in Mycobacterium vanbaalenii PYR1
    • Kim, S. J., O. Kweon, J. P. Freeman, R. C. Jones, M. D. Adjei, J. W. Jhoo, R. D. Edmondson, and C. E. Cerniglia. 2006. Molecular cloning and expression of genes encoding a novel dioxygenase involved in lowand high-molecular-weight polycyclic aromatic hydrocarbon degradation in Mycobacterium vanbaalenii PYR1. Appl. Environ. Microbiol. 72: 1045-1054.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 1045-1054
    • Kim, S.J.1    Kweon, O.2    Freeman, J.P.3    Jones, R.C.4    Adjei, M.D.5    Jhoo, J.W.6    Edmondson, R.D.7    Cerniglia, C.E.8
  • 12
    • 33846251226 scopus 로고    scopus 로고
    • Complete and integrated pyrene degradation pathway in Mycobacterium vanbaalenii PYR-1 based on systems biology
    • Kim, S. J., O. Kweon, R. C. Jones, J. P. Freeman, R. D. Edmondson, and C. E. Cerniglia. 2007. Complete and integrated pyrene degradation pathway in Mycobacterium vanbaalenii PYR-1 based on systems biology. J. Bacteriol. 189:464-472.
    • (2007) J. Bacteriol. , vol.189 , pp. 464-472
    • Kim, S.J.1    Kweon, O.2    Jones, R.C.3    Freeman, J.P.4    Edmondson, R.D.5    Cerniglia, C.E.6
  • 13
    • 34347401651 scopus 로고    scopus 로고
    • A polyomic approach to elucidate the fluoranthene degradative pathway in Mycobacterium vanbaalenii PYR-1
    • Kweon, O., S. J. Kim, R. C. Jones, J. P. Freeman, M. D. Adjei, R. D. Edmondson, and C. E. Cerniglia. 2007. A polyomic approach to elucidate the fluoranthene degradative pathway in Mycobacterium vanbaalenii PYR-1. J. Bacteriol. 189:4635-4647.
    • (2007) J. Bacteriol. , vol.189 , pp. 4635-4647
    • Kweon, O.1    Kim, S.J.2    Jones, R.C.3    Freeman, J.P.4    Adjei, M.D.5    Edmondson, R.D.6    Cerniglia, C.E.7
  • 14
    • 52749087095 scopus 로고    scopus 로고
    • Genomic analysis of polycyclic aromatic hydrocarbon degradation in Mycobacterium vanbaalenii PYR-1
    • Kim, S. J., O. Kweon, R. C. Jones, R. D. Edmondson, and C. E. Cerniglia. 2008. Genomic analysis of polycyclic aromatic hydrocarbon degradation in Mycobacterium vanbaalenii PYR-1. Biodegradation 19: 859-881.
    • (2008) Biodegradation , vol.19 , pp. 859-881
    • Kim, S.J.1    Kweon, O.2    Jones, R.C.3    Edmondson, R.D.4    Cerniglia, C.E.5
  • 15
    • 0035432965 scopus 로고    scopus 로고
    • Molecular cloning, nucleotide sequence, and expression of genes encoding a polycyclic aromatic ring dioxygenase from Mycobacterium sp. strain PYR-1
    • Khan, A. A., R. F. Wang, W. W. Cao, D. R. Doerge, D. Wennerstrom, and C. E. Cerniglia. 2001. Molecular cloning, nucleotide sequence, and expression of genes encoding a polycyclic aromatic ring dioxygenase from Mycobacterium sp. strain PYR-1. Appl. Environ. Microbiol. 67: 3577-3585.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 3577-3585
    • Khan, A.A.1    Wang, R.F.2    Cao, W.W.3    Doerge, D.R.4    Wennerstrom, D.5    Cerniglia, C.E.6
  • 16
    • 66349136181 scopus 로고    scopus 로고
    • Proteomic applications to elucidate bacterial aromatic hydrocarbon metabolic pathways
    • Kim, S. J., O. Kweon, and C. E. Cerniglia. 2009. Proteomic applications to elucidate bacterial aromatic hydrocarbon metabolic pathways. Curr. Opin. Microbiol. 12:301-309.
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 301-309
    • Kim, S.J.1    Kweon, O.2    Cerniglia, C.E.3
  • 17
    • 33847400228 scopus 로고    scopus 로고
    • Isolation and characterization of a gene cluster involved in PAH degradation in Mycobacterium sp. strain SNP11: Expression in Mycobacterium smegmatis mc2155
    • Pagnout, C., G. Frache, P. Poupin, B. Maunit, J. F. Muller, and J. F. Ferard. 2007. Isolation and characterization of a gene cluster involved in PAH degradation in Mycobacterium sp. strain SNP11: expression in Mycobacterium smegmatis mc2155. Res. Microbiol. 158:175-186.
    • (2007) Res. Microbiol. , vol.158 , pp. 175-186
    • Pagnout, C.1    Frache, G.2    Poupin, P.3    Maunit, B.4    Muller, J.F.5    Ferard, J.F.6
  • 18
    • 0037701540 scopus 로고    scopus 로고
    • Identification of pyrene-induced proteins in Mycobacterium sp. strain 6PY1: Evidence for two ring-hydroxylating dioxygenases
    • Krivobok, S., S. Kuony, C. Meyer, M. Louwagie, J. C. Willison, and Y. Jouanneau. 2003. Identification of pyrene-induced proteins in Mycobacterium sp. strain 6PY1: evidence for two ring-hydroxylating dioxygenases. J. Bacteriol. 185:3828-3841.
    • (2003) J. Bacteriol. , vol.185 , pp. 3828-3841
    • Krivobok, S.1    Kuony, S.2    Meyer, C.3    Louwagie, M.4    Willison, J.C.5    Jouanneau, Y.6
  • 19
    • 8744268521 scopus 로고    scopus 로고
    • Identification and functional analysis of two aromatic-ring-hydroxylating dioxygenases from a Sphingomonas strain that degrades various polycyclic aromatic hydrocarbons
    • Demanèche, S., C. Meyer, J. Micoud, M. Louwagie, J. C. Willison, and Y. Jouanneau. 2004. Identification and functional analysis of two aromatic-ring-hydroxylating dioxygenases from a Sphingomonas strain that degrades various polycyclic aromatic hydrocarbons. Appl. Environ. Microbiol. 70:6714-6725.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 6714-6725
    • Demanèche, S.1    Meyer, C.2    Micoud, J.3    Louwagie, M.4    Willison, J.C.5    Jouanneau, Y.6
  • 20
    • 9644286057 scopus 로고    scopus 로고
    • Isolation and characterization of polycyclic aromatic hydrocarbon-degrading Mycobacterium isolates from soil
    • Miller, C. D., K. Hall, Y. N. Liang, K. Nieman, D. Sorensen, B. Issa, A. J. Anderson, and R. C. Sims. 2004. Isolation and characterization of polycyclic aromatic hydrocarbon-degrading Mycobacterium isolates from soil. Microb. Ecol. 48:230-238.
    • (2004) Microb. Ecol. , vol.48 , pp. 230-238
    • Miller, C.D.1    Hall, K.2    Liang, Y.N.3    Nieman, K.4    Sorensen, D.5    Issa, B.6    Anderson, A.J.7    Sims, R.C.8
  • 21
    • 2142695718 scopus 로고    scopus 로고
    • Two distinct gene clusters encode pyrene degradation in Mycobacterium sp. strain S65
    • Sho, M., C. Hamel, and C. W. Greer. 2004. Two distinct gene clusters encode pyrene degradation in Mycobacterium sp. strain S65. FEMS Microbiol. Ecol. 48:209-220.
    • (2004) FEMS Microbiol. Ecol. , vol.48 , pp. 209-220
    • Sho, M.1    Hamel, C.2    Greer, C.W.3
  • 22
    • 34547674725 scopus 로고    scopus 로고
    • Comparative quantitative prevalence of mycobacteria and functionally abundant nidA, nahAc, and nagAc dioxygenase genes in coal tar contaminated sediments
    • Debruyn, J. M., C. S. Chewning, and G. S. Sayler. 2007. Comparative quantitative prevalence of mycobacteria and functionally abundant nidA, nahAc, and nagAc dioxygenase genes in coal tar contaminated sediments. Environ. Sci. Technol. 41:5426-5432.
    • (2007) Environ. Sci. Technol. , vol.41 , pp. 5426-5432
    • Debruyn, J.M.1    Chewning, C.S.2    Sayler, G.S.3
  • 23
    • 42249095068 scopus 로고    scopus 로고
    • Realtime PCR quantification of PAH-ring hydroxylating dioxygenase (PAHRHDalpha) genes from Gram positive and Gram negative bacteria in soil and sediment samples
    • Cébron, A., M. P. Norini, T. Beguiristain, and C. Leyval. 2008. Realtime PCR quantification of PAH-ring hydroxylating dioxygenase (PAHRHDalpha) genes from Gram positive and Gram negative bacteria in soil and sediment samples. J. Microbiol. Methods 73:148-159.
    • (2008) J. Microbiol. Methods , vol.73 , pp. 148-159
    • Cébron, A.1    Norini, M.P.2    Beguiristain, T.3    Leyval, C.4
  • 24
    • 0038317584 scopus 로고    scopus 로고
    • Characterization of hydrocarbon-degrading microbial populations in contaminated and pristine alpine soils
    • Margesin, R., D. Labbe, F. Schinner, C. W. Greer, and L. G. Whyte. 2003. Characterization of hydrocarbon-degrading microbial populations in contaminated and pristine alpine soils. Appl. Environ. Microbiol. 69: 3085-3092.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 3085-3092
    • Margesin, R.1    Labbe, D.2    Schinner, F.3    Greer, C.W.4    Whyte, L.G.5
  • 25
    • 43149093388 scopus 로고    scopus 로고
    • A new classification system for bacterial Rieske non-heme iron aromatic ring-hydroxylating oxygenases
    • Kweon, O., S. J. Kim, S. Baek, J. C. Chae, M. D. Adjei, D. H. Baek, Y. C. Kim, and C. E. Cerniglia. 2008. A new classification system for bacterial Rieske non-heme iron aromatic ring-hydroxylating oxygenases. BMC Biochem. 9:11.
    • (2008) BMC Biochem. , vol.9 , pp. 11
    • Kweon, O.1    Kim, S.J.2    Baek, S.3    Chae, J.C.4    Adjei, M.D.5    Baek, D.H.6    Kim, Y.C.7    Cerniglia, C.E.8
  • 26
    • 4143146355 scopus 로고    scopus 로고
    • Molecular characterization of a phenanthrene degradation pathway in Mycobacterium vanbaalenii PYR1
    • Stingley, R. L., A. A. Khan, and C. E. Cerniglia. 2004. Molecular characterization of a phenanthrene degradation pathway in Mycobacterium vanbaalenii PYR1. Biochem. Biophys. Res. Commun. 322:133-146.
    • (2004) Biochem. Biophys. Res. Commun. , vol.322 , pp. 133-146
    • Stingley, R.L.1    Khan, A.A.2    Cerniglia, C.E.3
  • 27
    • 0034034019 scopus 로고    scopus 로고
    • A novel phenanthrene dioxygenase from Nocardioides sp. strain KP7: Expression in Escherichia coli
    • Saito, A., T. Iwabuchi, and S. Harayama. 2000. A novel phenanthrene dioxygenase from Nocardioides sp. strain KP7: expression in Escherichia coli. J. Bacteriol. 182:2134-2141.
    • (2000) J. Bacteriol. , vol.182 , pp. 2134-2141
    • Saito, A.1    Iwabuchi, T.2    Harayama, S.3
  • 28
    • 27144495787 scopus 로고    scopus 로고
    • Structure and increased thermostability of Rhodococcus sp. naphthalene 1,2-dioxygenase
    • Gakhar, L., Z. A. Malik, C. C. Allen, D. A. Lipscomb, M. J. Larkin, and S. Ramaswamy. 2005. Structure and increased thermostability of Rhodococcus sp. naphthalene 1,2-dioxygenase. J. Bacteriol. 187:7222-7231.
    • (2005) J. Bacteriol. , vol.187 , pp. 7222-7231
    • Gakhar, L.1    Malik, Z.A.2    Allen, C.C.3    Lipscomb, D.A.4    Larkin, M.J.5    Ramaswamy, S.6
  • 30
    • 33749528170 scopus 로고    scopus 로고
    • Characterization of a naphthalene dioxygenase endowed with an exceptionally broad substrate specificity toward polycyclic aromatic hydrocarbons
    • Jouanneau, Y., C. Meyer, J. Jakoncic, V. Stojanoff, and J. Gaillard. 2006. Characterization of a naphthalene dioxygenase endowed with an exceptionally broad substrate specificity toward polycyclic aromatic hydrocarbons. Biochemistry 45:12380-12391.
    • (2006) Biochemistry , vol.45 , pp. 12380-12391
    • Jouanneau, Y.1    Meyer, C.2    Jakoncic, J.3    Stojanoff, V.4    Gaillard, J.5
  • 31
    • 0024295005 scopus 로고
    • Benzylic monooxygenation catalyzed by toluene dioxygenase from Pseudomonas putida
    • Wackett, L. P., L. D. Kwart, and D. T. Gibson. 1988. Benzylic monooxygenation catalyzed by toluene dioxygenase from Pseudomonas putida. Biochemistry 27:1360-1367.
    • (1988) Biochemistry , vol.27 , pp. 1360-1367
    • Wackett, L.P.1    Kwart, L.D.2    Gibson, D.T.3
  • 32
    • 0029090715 scopus 로고
    • Stereospecific sulfoxidation by toluene and naphthalene dioxygenases
    • Lee, K., J. M. Brand, and D. T. Gibson. 1995. Stereospecific sulfoxidation by toluene and naphthalene dioxygenases. Biochem. Biophys. Res. Commun. 212:9-15.
    • (1995) Biochem. Biophys. Res. Commun. , vol.212 , pp. 9-15
    • Lee, K.1    Brand, J.M.2    Gibson, D.T.3
  • 33
    • 33746916823 scopus 로고    scopus 로고
    • A molecular modeling analysis of polycyclic aromatic hydrocarbon biodegradation by naphthalene dioxygenase
    • Wammer, K. H., and C. A. Peters. 2006. A molecular modeling analysis of polycyclic aromatic hydrocarbon biodegradation by naphthalene dioxygenase. Environ. Toxicol. Chem. 25:912-920.
    • (2006) Environ. Toxicol. Chem. , vol.25 , pp. 912-920
    • Wammer, K.H.1    Peters, C.A.2
  • 34
    • 33845483902 scopus 로고    scopus 로고
    • The catalytic pocket of the ring-hydroxylating dioxygenase from Sphingomonas CHY-1
    • Jakoncic, J., Y. Jouanneau, C. Meyer, and V. Stojanoff. 2007. The catalytic pocket of the ring-hydroxylating dioxygenase from Sphingomonas CHY-1. Biochem. Biophys. Res. Commun. 352:861-866.
    • (2007) Biochem. Biophys. Res. Commun. , vol.352 , pp. 861-866
    • Jakoncic, J.1    Jouanneau, Y.2    Meyer, C.3    Stojanoff, V.4
  • 35
    • 34047222146 scopus 로고    scopus 로고
    • Structural investigations of the ferredoxin and terminal oxygenase components of the biphenyl 2,3-dioxygenase from Sphingobium yanoikuyae B1
    • Ferraro, D. J., E. N. Brown, C. L. Yu, R. E. Parales, D. T. Gibson, and S. Ramaswamy. 2007. Structural investigations of the ferredoxin and terminal oxygenase components of the biphenyl 2,3-dioxygenase from Sphingobium yanoikuyae B1. BMC Struct. Biol. 7:10.
    • (2007) BMC Struct. Biol. , vol.7 , pp. 10
    • Ferraro, D.J.1    Brown, E.N.2    Yu, C.L.3    Parales, R.E.4    Gibson, D.T.5    Ramaswamy, S.6
  • 36
    • 27544477399 scopus 로고    scopus 로고
    • Rieske business: Structure-function of Rieske non-heme oxygenases
    • Ferraro, D. J., L. Gakhar, and S. Ramaswamy. 2005. Rieske business: structure-function of Rieske non-heme oxygenases. Biochem. Biophys. Res. Commun. 338:175-190.
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 175-190
    • Ferraro, D.J.1    Gakhar, L.2    Ramaswamy, S.3
  • 37
    • 0037826062 scopus 로고    scopus 로고
    • The role of active-site residues in naphthalene dioxygenase
    • Parales, R. E. 2003. The role of active-site residues in naphthalene dioxygenase. J. Ind. Microbiol. Biotechnol. 30:271-278.
    • (2003) J. Ind. Microbiol. Biotechnol. , vol.30 , pp. 271-278
    • Parales, R.E.1
  • 38
    • 0034051818 scopus 로고    scopus 로고
    • Substrate specificity of naphthalene dioxygenase: Effect of specific amino acids at the active site of the enzyme
    • Parales, R. E., K. Lee, S. M. Resnick, H. Jiang, D. J. Lessner, and D. T. Gibson. 2000. Substrate specificity of naphthalene dioxygenase: effect of specific amino acids at the active site of the enzyme. J. Bacteriol. 182: 1641-1649.
    • (2000) J. Bacteriol. , vol.182 , pp. 1641-1649
    • Parales, R.E.1    Lee, K.2    Resnick, S.M.3    Jiang, H.4    Lessner, D.J.5    Gibson, D.T.6
  • 39
    • 0033797753 scopus 로고    scopus 로고
    • Regioselectivity and enantioselectivity of naphthalene dioxygenase during arene cis-dihydroxylation: Control by phenylalanine 352 in the alpha subunit
    • Parales, R. E., S. M. Resnick, C. L. Yu, D. R. Boyd, N. D. Sharma, and D. T. Gibson. 2000. Regioselectivity and enantioselectivity of naphthalene dioxygenase during arene cis-dihydroxylation: control by phenylalanine 352 in the alpha subunit. J. Bacteriol. 182:5495-5504.
    • (2000) J. Bacteriol. , vol.182 , pp. 5495-5504
    • Parales, R.E.1    Resnick, S.M.2    Yu, C.L.3    Boyd, D.R.4    Sharma, N.D.5    Gibson, D.T.6
  • 40
    • 33749347047 scopus 로고    scopus 로고
    • Structural basis for regioselectivity and stereoselectivity of product formation by naphthalene 1,2-dioxygenase
    • Ferraro, D. J., A. L. Okerlund, J. C. Mowers, and S. Ramaswamy. 2006. Structural basis for regioselectivity and stereoselectivity of product formation by naphthalene 1,2-dioxygenase. J. Bacteriol. 188:6986-6994.
    • (2006) J. Bacteriol. , vol.188 , pp. 6986-6994
    • Ferraro, D.J.1    Okerlund, A.L.2    Mowers, J.C.3    Ramaswamy, S.4
  • 41
    • 4444337310 scopus 로고    scopus 로고
    • Crystal structure of the terminal oxygenase component of biphenyl dioxygenase derived from Rhodococcus sp. strain RHA1
    • Furusawa, Y., V. Nagarajan, M. Tanokura, E. Masai, M. Fukuda, and T. Senda. 2004 Crystal structure of the terminal oxygenase component of biphenyl dioxygenase derived from Rhodococcus sp. strain RHA1. J. Mol. Biol. 342:1041-1052.
    • (2004) J. Mol. Biol. , vol.342 , pp. 1041-1052
    • Furusawa, Y.1    Nagarajan, V.2    Tanokura, M.3    Masai, E.4    Fukuda, M.5    Senda, T.6
  • 42
    • 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
  • 43
    • 0034480510 scopus 로고    scopus 로고
    • A cluster exposed: Structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins
    • Colbert, C. L., M. M. Couture, L. D. Eltis, and J. T. Bolin. 2000. A cluster exposed: structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins. Structure 8:1267-1278.
    • (2000) Structure , vol.8 , pp. 1267-1278
    • Colbert, C.L.1    Couture, M.M.2    Eltis, L.D.3    Bolin, J.T.4
  • 44
    • 24944529052 scopus 로고    scopus 로고
    • Metabolic regio- and stereoselectivity of cytochrome P450 2D6 towards 3,4-methylenedioxy-N-alkylamphetamines: In silico predictions and experimental validation
    • Keizers, P. H., C. de Graaf, F. J. de Kanter, C. Oostenbrink, K. A. Feenstra, J. N. Commandeur, and N. P. Vermeulen. 2005. Metabolic regio- and stereoselectivity of cytochrome P450 2D6 towards 3,4-methylenedioxy-N-alkylamphetamines: in silico predictions and experimental validation. J. Med. Chem. 48:6117-6127.
    • (2005) J. Med. Chem. , vol.48 , pp. 6117-6127
    • Keizers, P.H.1    de Graaf, C.2    de Kanter, F.J.3    Oostenbrink, C.4    Feenstra, K.A.5    Commandeur, J.N.6    Vermeulen, N.P.7
  • 45
    • 0037058831 scopus 로고    scopus 로고
    • Role of protein and substrate dynamics in catalysis by Pseudomonas putida cytochrome P450cam
    • Prasad, S., and S. Mitra. 2002. Role of protein and substrate dynamics in catalysis by Pseudomonas putida cytochrome P450cam. Biochemistry 41: 14499-14508.
    • (2002) Biochemistry , vol.41 , pp. 14499-14508
    • Prasad, S.1    Mitra, S.2
  • 46
    • 0042168976 scopus 로고    scopus 로고
    • Two polycyclic aromatic hydrocarbon o-quinone reductases from a pyrene-degrading Mycobacterium
    • Kim, Y. H., K. H. Engesser, and C. E. Cerniglia. 2003. Two polycyclic aromatic hydrocarbon o-quinone reductases from a pyrene-degrading Mycobacterium. Arch. Biochem. Biophys. 416:209-217.
    • (2003) Arch. Biochem. Biophys. , vol.416 , pp. 209-217
    • Kim, Y.H.1    Engesser, K.H.2    Cerniglia, C.E.3
  • 47
    • 0035729093 scopus 로고    scopus 로고
    • Bacterial degradation of aromatic compounds via angular dioxygenation
    • Nojiri, H., H. Habe, and T. Omori. 2001. Bacterial degradation of aromatic compounds via angular dioxygenation. J. Gen. Appl. Microbiol. 47:279-305.
    • (2001) J. Gen. Appl. Microbiol. , vol.47 , pp. 279-305
    • Nojiri, H.1    Habe, H.2    Omori, T.3
  • 48
    • 0034084433 scopus 로고    scopus 로고
    • Bacterial metabolism of fluorene, dibenzofuran, dibenzothiophene, and carbazole
    • Bressler, D. C., and P. M. Fedorak. 2000 Bacterial metabolism of fluorene, dibenzofuran, dibenzothiophene, and carbazole. Can. J. Microbiol. 46:397-409.
    • (2000) Can. J. Microbiol. , vol.46 , pp. 397-409
    • Bressler, D.C.1    Fedorak, P.M.2
  • 49
    • 0042622380 scopus 로고    scopus 로고
    • SWISSMODEL: An automated protein homology-modeling server
    • Schwede, T., J. Kopp, N. Guex, and M. C. Peitsch. 2003. SWISSMODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31:3381-3385.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 51
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace, A. C., R. A. Laskowski, and J. M. Thornton. 1995. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8:127-134.
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 52
    • 33747818007 scopus 로고    scopus 로고
    • CASTp: Computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
    • Dundas, J., Z. Ouyang, J. Tseng, A. Binkowski, Y. Turpaz, and J. Liang. 2006. CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues. Nucleic Acids Res. 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
  • 53
    • 42449090264 scopus 로고    scopus 로고
    • PROMALS3D: A tool for multiple protein sequence and structure alignments
    • Pei, J., B. H. Kim, and N. V. Grishin. 2008. PROMALS3D: a tool for multiple protein sequence and structure alignments. Nucleic Acids Res. 36:2295-2300.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 2295-2300
    • Pei, J.1    Kim, B.H.2    Grishin, N.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.