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Volumn 274, Issue 10, 2007, Pages 2470-2481

The crystal structure of the ring-hydroxylating dioxygenase from Sphingomonas CHY-1

Author keywords

Bioremediation; Crystal structure; Heavy molecular weight polycyclic aromatic hydrocarbons; Rieske non heme iron oxygenase

Indexed keywords

BACTERIAL ENZYME; DIOXYGENASE; IRON OXYGENASE; OXYGENASE; POLYCYCLIC AROMATIC HYDROCARBON; RING HYDROXYLATING DIOXYGENASE; UNCLASSIFIED DRUG;

EID: 34247578182     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.05783.x     Document Type: Article
Times cited : (46)

References (39)
  • 1
    • 0033884282 scopus 로고    scopus 로고
    • Bioremediation of high molecular weight polycyclic aromatic hydrocarbons: A review of the microbial degradation of benzo[a]pyrene
    • Juhasz AL Naidu R (2000) Bioremediation of high molecular weight polycyclic aromatic hydrocarbons: a review of the microbial degradation of benzo[a]pyrene. Int Biodet Biodegr 45, 57 88.
    • (2000) Int Biodet Biodegr , vol.45 , pp. 57-88
    • Juhasz, A.L.1    Naidu, R.2
  • 2
    • 0034110781 scopus 로고    scopus 로고
    • Biodegradation of high-molecular-weight polycyclic aromatic hydrocarbons by bacteria
    • Kanaly R Harayama S (2000) Biodegradation of high-molecular-weight polycyclic aromatic hydrocarbons by bacteria J Bacteriol 182, 2059 2067.
    • (2000) J Bacteriol , vol.182 , pp. 2059-2067
    • Kanaly, R.1    Harayama, S.2
  • 3
    • 0016861706 scopus 로고
    • Oxidation of the carcinogens benzo[a]pyrene and benzo[a]anthracene to dihydrodiols by a bacterium
    • Gibson DT, Mahadevan V, Jerina DM, Yogi H Yeh HJ (1975) Oxidation of the carcinogens benzo[a]pyrene and benzo[a]anthracene to dihydrodiols by a bacterium. Science 189, 295 297.
    • (1975) Science , vol.189 , pp. 295-297
    • Gibson, D.T.1    Mahadevan, V.2    Jerina, D.M.3    Yogi, H.4    Yeh, H.J.5
  • 4
  • 6
    • 0037701540 scopus 로고    scopus 로고
    • Identification of pyrene-induced proteins in Mycobacterium sp. Strain 6PY1: Evidence for two ring-hydroxylating dioxygenase
    • Krivobok S, Kuony S, Meyer C, Louwagie M, Willison JC Jouanneau Y (2003) Identification of pyrene-induced proteins in Mycobacterium sp. Strain 6PY1: evidence for two ring-hydroxylating dioxygenase 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
  • 7
    • 10444260518 scopus 로고    scopus 로고
    • Isolation and characterization of a novel sphingomonad capable of growth with chrysene as sole carbon and energy source
    • Willison JC (2004) Isolation and characterization of a novel sphingomonad capable of growth with chrysene as sole carbon and energy source. FEMS Microbiol Lett 241, 143 150.
    • (2004) FEMS Microbiol Lett , vol.241 , pp. 143-150
    • Willison, J.C.1
  • 8
    • 8744268521 scopus 로고    scopus 로고
    • Identification and functional analysis of two aromatic-ring-hydroxylating dioxygenases from a Spingomonas strain that degrades variuous polycyclic aromatic hydrocarbons
    • Demaneche S, Meyer C, Micoud J, Louwagie M, Willison JC Jouanneau Y (2004) Identification and functional analysis of two aromatic-ring-hydroxylating dioxygenases from a Spingomonas strain that degrades variuous polycyclic aromatic hydrocarbons. App Environ Microbiol 70, 6714 6725.
    • (2004) App Environ Microbiol , vol.70 , pp. 6714-6725
    • Demaneche, S.1    Meyer, C.2    Micoud, J.3    Louwagie, M.4    Willison, J.C.5    Jouanneau, Y.6
  • 9
    • 33749528170 scopus 로고    scopus 로고
    • Characterization of a ring-hydroxylating dioxygenase able to oxidize a wide range of polycyclic aromatic hydrocarbons including four and five ring carcinogens
    • Jouanneau Y, Meyer C, Jakoncic J, Stojanoff V Gaillard J (2006) Characterization of a ring-hydroxylating dioxygenase able to oxidize a wide range of polycyclic aromatic hydrocarbons including four and five ring carcinogens. 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
  • 10
    • 0029920974 scopus 로고    scopus 로고
    • The broad substrate chlorobenzene dioxygenase and cis-chlorobenzene dihydrodiol dehydrogenase of Pseudomonas sp. strain P51 are linked evolutionarily to the enzymes for benzene and toluene degradation
    • Werlen C, Kohler HPE van der Meer JR (1996) The broad substrate chlorobenzene dioxygenase and cis-chlorobenzene dihydrodiol dehydrogenase of Pseudomonas sp. strain P51 are linked evolutionarily to the enzymes for benzene and toluene degradation J Biol Chem 271, 4009 4016.
    • (1996) J Biol Chem , vol.271 , pp. 4009-4016
    • Werlen, C.1    Kohler, H.P.E.2    Van Der Meer, J.R.3
  • 14
  • 16
    • 4444337310 scopus 로고    scopus 로고
    • Crystal structure of the terminal oxygenase component of biphenyl dioxygenase derived from Rhodococcus sp. strain RHA1
    • Furusawa Y, Nagarajan V, Tanokura M, Masai E, Fukuda M Senda T (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
  • 18
    • 18944405592 scopus 로고    scopus 로고
    • 2-Oxoquinoline 8-monooxygenase oxygenase component: Active site modulation by Rieske-[2Fe-2S] center oxidation/reduction
    • Martins BM, Svetlitchnaia T Dobbek H (2005) 2-Oxoquinoline 8-monooxygenase oxygenase component: active site modulation by Rieske-[2Fe-2S] center oxidation/reduction Structure 13, 817 824.
    • (2005) Structure , vol.13 , pp. 817-824
    • Martins, B.M.1    Svetlitchnaia, T.2    Dobbek, H.3
  • 20
    • 0039302669 scopus 로고    scopus 로고
    • Dioxygen activation by enzymes with mononuclear non-heme iron active sites
    • Que JL Ho RYN (1996) Dioxygen activation by enzymes with mononuclear non-heme iron active sites. Chem Rev 96, 2607 2624.
    • (1996) Chem Rev , vol.96 , pp. 2607-2624
    • Que, J.L.1    Ho, R.Y.N.2
  • 21
    • 0031936811 scopus 로고    scopus 로고
    • Comparative studies of protein crystallization by vapour-diffusion and microbatch techniques
    • Chayen NE (1998) Comparative studies of protein crystallization by vapour-diffusion and microbatch techniques. Acta Cryst D54, 8 15.
    • (1998) Acta Cryst , vol.54 , pp. 8-15
    • Chayen, N.E.1
  • 23
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276, 307 326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 24
    • 0000560808 scopus 로고    scopus 로고
    • Molrep: An automated program for molecular replacement
    • Vagin A Teplyakov A (1997) molrep: an automated program for molecular replacement. J Appl Cryst 30, 1022 1025.
    • (1997) J Appl Cryst , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 25
    • 0002583957 scopus 로고
    • 'dm': An automated procedure for phase improvement by density modification
    • Cowtan K (1994) 'dm': An automated procedure for phase improvement by density modification. Joint CCP4 ESF-EACBM Newsletter Protein Crystallogr 31, 34 38.
    • (1994) Joint CCP4 ESF-EACBM Newsletter Protein Crystallogr , vol.31 , pp. 34-38
    • Cowtan, K.1
  • 26
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Mathews BW (1968) Solvent content of protein crystals. J Mol Biol 33, 491 497.
    • (1968) J Mol Biol , vol.33 , pp. 491-497
    • Mathews, B.W.1
  • 27
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A, Morris RM Lamzin VS (1999) Automated protein model building combined with iterative structure refinement. Nature Struct Biol 6, 458 463.
    • (1999) Nature Struct Biol , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.M.2    Lamzin, V.S.3
  • 28
    • 13244281317 scopus 로고    scopus 로고
    • Coot. Model-building tools for mol graphics
    • Emsley P Cowtan K (2004) coot. Model-building tools for mol graphics. Acta Cryst D60, 2126 2132.
    • (2004) Acta Cryst , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 29
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Cryst D53, 240 255.
    • (1997) Acta Cryst , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 30
    • 0000243829 scopus 로고
    • Procheck: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS Thornton JM (1993) procheck: a program to check the stereochemical quality of protein structures. J App Cryst 26, 283 291.
    • (1993) J App Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 31
    • 0037826062 scopus 로고    scopus 로고
    • The role of active site residues in naphthalene dioxygenase
    • Parales RE (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
  • 32
    • 33845483902 scopus 로고    scopus 로고
    • The catalytic pocket of the ring-hydroxylating dioxygenase from Sphingomonas CHY-1
    • Jakoncic J, Jouanneau Y, Meyer C Stojanoff V (2007) The catalytic pocket of the ring-hydroxylating dioxygenase from Sphingomonas CHY-1. Biochem Biophys Res Commun 352, 861 868.
    • (2007) Biochem Biophys Res Commun , vol.352 , pp. 861-868
    • Jakoncic, J.1    Jouanneau, Y.2    Meyer, C.3    Stojanoff, V.4
  • 33
    • 0032989253 scopus 로고    scopus 로고
    • Aspartate 205 in the catalytic domain of naphthalene dioxygenase is essential for activity
    • Parales RE, Parales JV Gibson DT (1999) Aspartate 205 in the catalytic domain of naphthalene dioxygenase is essential for activity J Bacteriol 181, 1831 1837.
    • (1999) J Bacteriol , vol.181 , pp. 1831-1837
    • Parales, R.E.1    Parales, J.V.2    Gibson, D.T.3
  • 34
    • 3042717031 scopus 로고    scopus 로고
    • A theoretical study of the cis-dihydroxylation mechanism in naphthalene 1,2-dioxygenase
    • Bassan A, Blomberg MR Siegbahn PE (2004) A theoretical study of the cis-dihydroxylation mechanism in naphthalene 1,2-dioxygenase J Biol Inorg Chem 9, 439 452.
    • (2004) J Biol Inorg Chem , vol.9 , pp. 439-452
    • Bassan, A.1    Blomberg, M.R.2    Siegbahn, P.E.3
  • 35
    • 0034051818 scopus 로고    scopus 로고
    • Substrate specificity of naphthalene dioxygenase: Effect of specific amino acids at the active site of the enzyme
    • Parales RE, Lee L, Resnick SM, Jiang H, Lessner DJ Gibson DT (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, L.2    Resnick, S.M.3    Jiang, H.4    Lessner, D.J.5    Gibson, D.T.6
  • 36
    • 0027968068 scopus 로고
    • Clustal w: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Higgins D, Thompson J, Gibson T, Thompson JD, Higgins DG Gibson TJ (1994) clustal w: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 224, 673 4680.
    • (1994) Nucleic Acids Res , vol.224 , pp. 673-4680
    • Higgins, D.1    Thompson, J.2    Gibson, T.3    Thompson, J.D.4    Higgins, D.G.5    Gibson, T.J.6
  • 37
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ (1991) molscript: a program to produce both detailed and schematic plots of protein structures. J Appl Cryst 24, 946 950.
    • (1991) J Appl Cryst , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 38
    • 0028057108 scopus 로고
    • Raster3d, Version 2.0: A program for photorealistic molecular graphics
    • Merritt EA Murphy ME (1994) raster3d, Version 2.0: a program for photorealistic molecular graphics. Acta Cryst D50, 869 873.
    • (1994) Acta Cryst , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.