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Volumn , Issue , 2014, Pages 181-205

Structure and function of aromatic-ring hydroxylating dioxygenase system

Author keywords

Aromatic ring; Crystal structure; Dioxygenation; Electron transfer; Hydroxylation; Nonheme iron; Protein protein interaction; Rieske oxygenase; Substrate specificity

Indexed keywords


EID: 84930905786     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-4-431-54520-0_9     Document Type: Chapter
Times cited : (6)

References (73)
  • 1
    • 0030789487 scopus 로고    scopus 로고
    • Molecular characterization of fdx1, a putidaredoxin-type [2fe-2s] ferredoxin able to transfer electrons to the dioxin dioxygenase of sphingomonas sp rw1
    • Armengaud J, Timmis KN. (1997). Molecular characterization of Fdx1, a putidaredoxin-type [2Fe-2S] ferredoxin able to transfer electrons to the dioxin dioxygenase of Sphingomonas sp. RW1. Eur J Biochem 247:833-842
    • (1997) Eur J Biochem , vol.247 , pp. 833-842
    • Armengaud, J.1    Timmis, K.N.2
  • 2
    • 0034127014 scopus 로고    scopus 로고
    • A second [2fe-2s] ferredoxin from sphingomonas sp strain rw1 can function as an electron donor for the dioxin dioxygenase
    • Armengaud J, Gaillard J, Timmis KN. (2000). A second [2Fe-2S] ferredoxin from Sphingomonas sp. Strain RW1 can function as an electron donor for the dioxin dioxygenase. J Bacteriol 182:2238-2244
    • (2000) J Bacteriol , vol.182 , pp. 2238-2244
    • Armengaud, J.1    Gaillard, J.2    Timmis, K.N.3
  • 3
    • 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. (2006). Electron transfer complex formation between oxygenase and ferredoxin components in Rieske nonheme iron oxygenase system. Structure 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
  • 4
    • 84862519842 scopus 로고    scopus 로고
    • Structural insight into the substrate-and dioxygen-binding manner in the catalytic cycle of rieske nonheme iron oxygenase system, carbazole 1,9a-dioxygenase
    • Ashikawa Y, Fujimoto Z, Usami Y, Inoue K, Noguchi H, Yamane H, Nojiri H. (2012). Structural insight into the substrate-and dioxygen-binding manner in the catalytic cycle of rieske nonheme iron oxygenase system, carbazole 1,9a-dioxygenase. BMC Struct Biol 12:15
    • (2012) BMC Struct Biol , vol.12 , pp. 15
    • Ashikawa, Y.1    Fujimoto, Z.2    Usami, Y.3    Inoue, K.4    Noguchi, H.5    Yamane, H.6    Nojiri, H.7
  • 6
    • 0344823655 scopus 로고    scopus 로고
    • Histidine ligand protonation and redox potential in the Rieske dioxygenases: Role of a conserved aspartate in anthranilate 1,2-dioxygenase
    • Beharry ZM, Eby DM, Coulter ED, Viswanathan R, Neidle EL, Phillips RS, Kurtz DM Jr. (2003). Histidine ligand protonation and redox potential in the Rieske dioxygenases: role of a conserved aspartate in anthranilate 1,2-dioxygenase. Biochemistry 42:13625-13636
    • (2003) Biochemistry , vol.42 , pp. 13625-13636
    • Beharry, Z.M.1    Eby, D.M.2    Coulter, E.D.3    Viswanathan, R.4    Neidle, E.L.5    Phillips, R.S.6    Kurtz, D.M.7
  • 7
    • 0031831881 scopus 로고    scopus 로고
    • The dioxygenase-catalysed formation of vicinal cis -diols
    • Boyd DR, Sheldrake GN. (1998). The Dioxygenase-catalysed formation of vicinal cis -diols. Nat Prod Rep 15:309-324
    • (1998) Nat Prod Rep , vol.15 , pp. 309-324
    • Boyd, D.R.1    Sheldrake, G.N.2
  • 9
    • 84862574311 scopus 로고    scopus 로고
    • Phylogenetic analysis reveals the surprising diversity of an oxygenase class
    • Capyk JK, Eltis LD. (2012). Phylogenetic analysis reveals the surprising diversity of an oxygenase class. J Biol Inorg Chem 17:425-436
    • (2012) J Biol Inorg Chem , vol.17 , pp. 425-436
    • Capyk, J.K.1    Eltis, L.D.2
  • 11
    • 0031574021 scopus 로고    scopus 로고
    • Biological identity and diversity in photosynthesis and respiration: Structure of the lumen-side domain of the chloroplast rieske protein
    • Carrell CJ, Zhang H, Cramer WA, Smith JL. (1997). Biological identity and diversity in photosynthesis and respiration: structure of the lumen-side domain of the chloroplast Rieske protein. Structure 5:1613-1625
    • (1997) Structure , vol.5 , pp. 1613-1625
    • Carrell, C.J.1    Zhang, H.2    Cramer, W.A.3    Smith, J.L.4
  • 13
    • 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 CL, Couture MM, Eltis LD, Bolin JT. (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
  • 14
    • 0027093793 scopus 로고
    • Phthalate dioxygenase reductase: A modular structure for electron transfer from pyridine nucleotides to [2fe-2s
    • Correll CC, Batie CJ, Ballou DP, Ludwig ML. (1992). Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S]. Science 258:1604-1610
    • (1992) Science , vol.258 , pp. 1604-1610
    • Correll, C.C.1    Batie, C.J.2    Ballou, D.P.3    Ludwig, M.L.4
  • 18
    • 69049107348 scopus 로고    scopus 로고
    • Crystal structure of dicamba monooxygenase: A Rieske nonheme oxygenase that catalyzes oxidative demethylation
    • Dumitru R, Jiang WZ, Weeks DP, Wilson MA. (2009). Crystal structure of dicamba monooxygenase: a Rieske nonheme oxygenase that catalyzes oxidative demethylation. J Mol Biol 392:498-510
    • (2009) J Mol Biol , vol.392 , pp. 498-510
    • Dumitru, R.1    Jiang, W.Z.2    Weeks, D.P.3    Wilson, M.A.4
  • 19
    • 33749347047 scopus 로고    scopus 로고
    • Structural basis for regioselectivity and stereoselectivity of product formation by naphthalene 1,2-dioxygenase
    • Ferraro DJ, Okerlund AL, Mowers JC, Ramaswamy S. (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
  • 20
    • 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 DJ, Brown EN, Yu CL, Parales RE, Gibson DT, Ramaswamy S. (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
  • 23
    • 3843075198 scopus 로고    scopus 로고
    • Biphenyl dioxygenases: Functional versatilities and directed evolution
    • Furukawa K, Suenaga H, Goto M. (2004). Biphenyl dioxygenases: functional versatilities and directed evolution. J Bacteriol 186:5189-5196
    • (2004) J Bacteriol , vol.186 , pp. 5189-5196
    • Furukawa, K.1    Suenaga, H.2    Goto, M.3
  • 24
    • 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
  • 25
  • 26
    • 0028792364 scopus 로고
    • Structure and mechanism of the iron-sulfur fl avoprotein phthalate dioxygenase reductase
    • Gassner GT, Ludwig ML, Gatti DL, Correll CC, Ballou DP. (1995). Structure and mechanism of the iron-sulfur fl avoprotein phthalate dioxygenase reductase. FASEB J 9:1411-1418
    • (1995) Faseb J , vol.9 , pp. 1411-1418
    • Gassner, G.T.1    Ludwig, M.L.2    Gatti, D.L.3    Correll, C.C.4    Ballou, D.P.5
  • 27
    • 0021378817 scopus 로고
    • An investigation of the iron-sulphur proteins of benzene dioxygenase from pseudomonas putida by electron-spin-resonance spectroscopy
    • Geary PJ, Saboowalla F, Patil D, Cammack R. (1984). An investigation of the iron-sulphur proteins of benzene dioxygenase from Pseudomonas putida by electron-spin-resonance spectroscopy. Biochem J 217:667-673
    • (1984) Biochem J , vol.217 , pp. 667-673
    • Geary, P.J.1    Saboowalla, F.2    Patil, D.3    Cammack, R.4
  • 28
    • 0034029015 scopus 로고    scopus 로고
    • Aromatic hydrocarbon dioxygenases in environmental biotechnology
    • Gibson DT, Parales RE. (2000). Aromatic hydrocarbon dioxygenases in environmental biotechnology. Curr Opin Biotechnol 11:236-243
    • (2000) Curr Opin Biotechnol , vol.11 , pp. 236-243
    • Gibson, D.T.1    Parales, R.E.2
  • 29
    • 0030891317 scopus 로고    scopus 로고
    • A novel suppressor of cell death in plants encoded by the lls1 gene of maize
    • Gray J, Close PS, Briggs SP, Johal GS. (1997). A novel suppressor of cell death in plants encoded by the Lls1 gene of maize. Cell 89:25-31
    • (1997) Cell , vol.89 , pp. 25-31
    • Gray, J.1    Close, P.S.2    Briggs, S.P.3    Johal, G.S.4
  • 31
    • 0031733410 scopus 로고    scopus 로고
    • Involvement of the terminal oxygenase beta subunit in the biphenyl dioxygenase reactivity pattern toward chlorobiphenyls
    • Hurtubise Y, Barriault D, Sylvestre M. (1998). Involvement of the terminal oxygenase beta subunit in the biphenyl dioxygenase reactivity pattern toward chlorobiphenyls. J Bacteriol 180:5828-5835
    • (1998) J Bacteriol , vol.180 , pp. 5828-5835
    • Hurtubise, Y.1    Barriault, D.2    Sylvestre, M.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. (2009). Specific interactions between the ferredoxin and terminal oxygenase components of a class IIB Rieske nonheme iron oxygenase, carbazole 1,9a-dioxygenase. J Mol Biol 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
    • 79958257334 scopus 로고    scopus 로고
    • Comparison of the specificities and efficacies of primers for aromatic dioxygenase gene analysis of environmental samples
    • Iwai S, Johnson TA, Chai B, Hashsham SA, Tiedje JM. (2011). Comparison of the specificities and efficacies of primers for aromatic dioxygenase gene analysis of environmental samples. Appl Environ Microbiol 77:3551-3557
    • (2011) Appl Environ Microbiol , vol.77 , pp. 3551-3557
    • Iwai, S.1    Johnson, T.A.2    Chai, B.3    Hashsham, S.A.4    Tiedje, J.M.5
  • 34
    • 0030585240 scopus 로고    scopus 로고
    • Structure of a water soluble fragment of the rieske iron-sulfur protein of the bovine heart mitochondrial cytochrome bc1 complex determined by mad phasing at 1.5 å resolution
    • Iwata S, Saynovits M, Link TA, Michel H. (1996). Structure of a water soluble fragment of the Rieske iron-sulfur protein of the bovine heart mitochondrial cytochrome bc1 complex determined by MAD phasing at 1.5 Å resolution. Structure 4:567-579
    • (1996) Structure , vol.4 , pp. 567-579
    • Iwata, S.1    Saynovits, M.2    Link, T.A.3    Michel, H.4
  • 35
    • 34247578182 scopus 로고    scopus 로고
    • The crystal structure of the ringhydroxylating dioxygenase from Sphingomonas CHY-1
    • Jakoncic J, Jouanneau Y, Meyer C, Stojanoff V. (2007). The crystal structure of the ringhydroxylating dioxygenase from Sphingomonas CHY-1. FEBS J 274:2470-2481
    • (2007) Febs J , vol.274 , pp. 2470-2481
    • Jakoncic, J.1    Jouanneau, Y.2    Meyer, C.3    Stojanoff, V.4
  • 36
    • 0029953163 scopus 로고    scopus 로고
    • Site-directed mutagenesis of conserved amino acids in the alpha subunit of toluene dioxygenase: Potential mononuclear non-heme iron coordination sites
    • Jiang H, Parales RE, Lynch NA, Gibson DT. (1996). Site-directed mutagenesis of conserved amino acids in the alpha subunit of toluene dioxygenase: potential mononuclear non-heme iron coordination sites. J Bacteriol 178:3133-3139
    • (1996) J Bacteriol , vol.178 , pp. 3133-3139
    • Jiang, H.1    Parales, R.E.2    Lynch, N.A.3    Gibson, D.T.4
  • 41
    • 33144467842 scopus 로고    scopus 로고
    • Molecular cloning and expression of genes encoding a novel dioxygenase involved in low-and high-molecular-weight polycyclic aromatic hydrocarbon degradation in mycobacterium vanbaalenii pyr-1
    • Kim SJ, Kweon O, Freeman JP, Jones RC, Adjei MD, Jhoo JW, Edmondson RD, Cerniglia CE. (2006). Molecular cloning and expression of genes encoding a novel dioxygenase involved in low-and high-molecular-weight polycyclic aromatic hydrocarbon degradation in Mycobacterium vanbaalenii PYR-1. 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
  • 42
    • 4744343780 scopus 로고    scopus 로고
    • Negatively charged residues and hydrogen bonds tune the ligand histidine pKa values of Rieske iron-sulfur proteins
    • Klingen AR, Ullmann GM. (2004). Negatively charged residues and hydrogen bonds tune the ligand histidine pKa values of Rieske iron-sulfur proteins. Biochemistry 43:12383-12389
    • (2004) Biochemistry , vol.43 , pp. 12383-12389
    • Klingen, A.R.1    Ullmann, G.M.2
  • 43
    • 39449130475 scopus 로고    scopus 로고
    • Versatility of biological non-heme fe(ii) centers in oxygen activation reactions
    • Kovaleva EG, Lipscomb JD. (2008). Versatility of biological non-heme Fe(II) centers in oxygen activation reactions. Nat Chem Biol 4:186-193
    • (2008) Nat Chem Biol , vol.4 , pp. 186-193
    • Kovaleva, E.G.1    Lipscomb, J.D.2
  • 44
    • 0031874757 scopus 로고    scopus 로고
    • Enhanced degradation of polychlorinated biphenyls by directed evolution of biphenyl dioxygenase
    • Kumamaru T, Suenaga H, Mitsuoka M, Watanabe T, Furukawa K. (1998). Enhanced degradation of polychlorinated biphenyls by directed evolution of biphenyl dioxygenase. Nat Biotechnol 16:663-666
    • (1998) Nat Biotechnol , vol.16 , pp. 663-666
    • Kumamaru, T.1    Suenaga, H.2    Mitsuoka, M.3    Watanabe, T.4    Furukawa, K.5
  • 47
    • 0032929306 scopus 로고    scopus 로고
    • A novel aromatic-ring-hydroxylating dioxygenase from the diterpenoid-degrading bacterium pseudomonas abietaniphila bkme-9
    • Martin VJ, Mohn WW. (1999). A novel aromatic-ring-hydroxylating dioxygenase from the diterpenoid-degrading bacterium Pseudomonas abietaniphila BKME-9. J Bacteriol 181: 2675-2682
    • (1999) J Bacteriol , vol.181 , pp. 2675-2682
    • Martin, V.J.1    Mohn, W.W.2
  • 48
    • 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
  • 51
    • 34447326187 scopus 로고    scopus 로고
    • Hydrogen peroxide dependent cis-dihydroxylation of benzoate by fully oxidized benzoate 1,2-dioxygenase
    • Neibergall MB, Stubna A, Mekmouche Y, Munck E, Lipscomb JD. (2007). Hydrogen peroxide dependent cis-dihydroxylation of benzoate by fully oxidized benzoate 1,2-dioxygenase. Biochemistry 46:8004-8016
    • (2007) Biochemistry , vol.46 , pp. 8004-8016
    • Neibergall, M.B.1    Stubna, A.2    Mekmouche, Y.3    Munck, E.4    Lipscomb, J.D.5
  • 52
    • 84856606092 scopus 로고    scopus 로고
    • Structural and molecular genetic analyses of the bacterial carbazole degradation system
    • Nojiri H. (2012). Structural and molecular genetic analyses of the bacterial carbazole degradation system. Biosci Biotechnol Biochem 76:1-18
    • (2012) Biosci Biotechnol Biochem , vol.76 , pp. 1-18
    • Nojiri, H.1
  • 54
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • Page CC, Moser CC, Chen X, Dutton PL. (1999). Natural engineering principles of electron tunnelling in biological oxidation-reduction. Nature 402:47-52
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.3    Dutton, P.L.4
  • 55
    • 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 K, Resnick SM, Jiang H, Lessner DJ, Gibson DT. (2000a). 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
  • 56
    • 0033797753 scopus 로고    scopus 로고
    • Regioselectivity and enantioselectivity of naphthalene dioxygenase during arene cis -dihydroxylation: Control by phenylalanine 352 in the alpha subunit
    • Parales RE, Resnick SM, Yu CL, Boyd DR, Sharma ND, Gibson DT. (2000b). 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
  • 57
    • 0029590773 scopus 로고
    • Epr, electron spin echo envelope modulation, and electron nuclear double resonance studies of the 2fe2s centers of the 2-halobenzoate 1,2-dioxygenase from burkholderia (pseudomonas) cepacia 2cbs
    • Riedel A, Fetzner S, Rampp M, Lingens F, Liebl U, Zimmermann JL, Nitschke W. (1995). EPR, electron spin echo envelope modulation, and electron nuclear double resonance studies of the 2Fe2S centers of the 2-halobenzoate 1,2-dioxygenase from Burkholderia (Pseudomonas) cepacia 2CBS. J Biol Chem 270:30869-30873
    • (1995) J Biol Chem , vol.270 , pp. 30869-30873
    • Riedel, A.1    Fetzner, S.2    Rampp, M.3    Lingens, F.4    Liebl, U.5    Zimmermann, J.L.6    Nitschke, W.7
  • 58
    • 0028790887 scopus 로고
    • The 2Fe2S centres of the 2-oxo-1, 2-dihydroquinoline 8-monooxygenase from Pseudomonas putida 86 studied by EPR spectroscopy
    • Rosche B, Fetzner S, Lingens F, Nitschke W, Riedel A. (1995). The 2Fe2S centres of the 2-oxo-1, 2-dihydroquinoline 8-monooxygenase from Pseudomonas putida 86 studied by EPR spectroscopy. Biochim Biophys Acta 1252:177-179
    • (1995) Biochim Biophys Acta , vol.1252 , pp. 177-179
    • Rosche, B.1    Fetzner, S.2    Lingens, F.3    Nitschke, W.4    Riedel, A.5
  • 60
    • 34548836830 scopus 로고    scopus 로고
    • Molecular mechanism of the redox-dependent interaction between nadh-dependent ferredoxin reductase and riesketype [2fe-2s] ferredoxin
    • Senda M, Kishigami S, Kimura S, Fukuda M, Ishida T, Senda T. (2007). Molecular mechanism of the redox-dependent interaction between NADH-dependent ferredoxin reductase and Riesketype [2Fe-2S] ferredoxin. J Mol Biol 373:382-400
    • (2007) J Mol Biol , vol.373 , pp. 382-400
    • Senda, M.1    Kishigami, S.2    Kimura, S.3    Fukuda, M.4    Ishida, T.5    Senda, T.6
  • 61
    • 0021895134 scopus 로고
    • Purifi cation and properties of ferredoxin TOL. A component of toluene dioxygenase from Pseudomonas putida F1
    • Subramanian V, Liu TN, Yeh WK, Serdar CM, Wackett LP, Gibson DT. (1985). Purifi cation and properties of ferredoxin TOL. 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
  • 62
    • 0035933899 scopus 로고    scopus 로고
    • Emergence of multifunctional oxygenase activities by random priming recombination
    • Suenaga H, Goto M, Furukawa K. (2001). Emergence of multifunctional oxygenase activities by random priming recombination. J Biol Chem 276:22500-22506
    • (2001) J Biol Chem , vol.276 , pp. 22500-22506
    • Suenaga, H.1    Goto, M.2    Furukawa, K.3
  • 63
    • 0036285535 scopus 로고    scopus 로고
    • Alteration of regiospecificity in biphenyl dioxygenase by active-site engineering
    • Suenaga H, Watanabe T, Sato M, Ngadiman FK. (2002). Alteration of regiospecificity in biphenyl dioxygenase by active-site engineering. J Bacteriol 184:3682-3688
    • (2002) J Bacteriol , vol.184 , pp. 3682-3688
    • Suenaga, H.1    Watanabe, T.2    Sato, M.3    Ngadiman, F.K.4
  • 64
    • 23844520705 scopus 로고    scopus 로고
    • Characterization of [3fe-4s] ferredoxin dbfa3, which functions in the angular dioxygenase system of terrabacter sp strain dbf63
    • Takagi T, Habe H, Yoshida T, Yamane H, Omori T, Nojiri H. (2005). Characterization of [3Fe-4S] ferredoxin DbfA3, which functions in the angular dioxygenase system of Terrabacter sp. strain DBF63. Appl Microbiol Biotechnol 68:336-345
    • (2005) Appl Microbiol Biotechnol , vol.68 , pp. 336-345
    • Takagi, T.1    Habe, H.2    Yoshida, T.3    Yamane, H.4    Omori, T.5    Nojiri, H.6
  • 65
    • 0032514698 scopus 로고    scopus 로고
    • Chlorophyll a oxygenase (cao) is involved in chlorophyll b formation from chlorophyll a
    • Tanaka A, Ito H, Tanaka R, Tanaka NK, Yoshida K, Okada K. (1998). Chlorophyll a oxygenase (CAO) is involved in chlorophyll b formation from chlorophyll a . Proc Natl Acad Sci USA 95:12719-12723
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12719-12723
    • Tanaka, A.1    Ito, H.2    Tanaka, R.3    Tanaka, N.K.4    Yoshida, K.5    Okada, K.6
  • 67
    • 33846979487 scopus 로고    scopus 로고
    • Enzymatic hydroxylation of aromatic compounds
    • Ullrich R, Hofrichter M. (2007). Enzymatic hydroxylation of aromatic compounds. Cell Mol Life Sci 64:271-293
    • (2007) Cell Mol Life Sci , vol.64 , pp. 271-293
    • Ullrich, R.1    Hofrichter, M.2
  • 68
    • 0037428401 scopus 로고    scopus 로고
    • Hydrogen peroxide-coupled cis -diol formation catalyzed by naphthalene 1,2-dioxygenase
    • Wolfe MD, Lipscomb JD. (2003). Hydrogen peroxide-coupled cis -diol formation catalyzed by naphthalene 1,2-dioxygenase. J Biol Chem 278:829-835
    • (2003) J Biol Chem , vol.278 , pp. 829-835
    • Wolfe, M.D.1    Lipscomb, J.D.2
  • 69
    • 0035910409 scopus 로고    scopus 로고
    • Single turnover chemistry and regulation of O 2 activation by the oxygenase component of naphthalene 1,2-dioxygenase
    • Wolfe MD, Parales JV, Gibson DT, Lipscomb JD. (2001). Single turnover chemistry and regulation of O 2 activation by the oxygenase component of naphthalene 1,2-dioxygenase. J Biol Chem 276:1945-1953
    • (2001) J Biol Chem , vol.276 , pp. 1945-1953
    • Wolfe, M.D.1    Parales, J.V.2    Gibson, D.T.3    Lipscomb, J.D.4
  • 70
    • 0037199485 scopus 로고    scopus 로고
    • Benzoate 1,2-dioxygenase from pseudomonas putida: Single turnover kinetics and regulation of a twocomponent rieske dioxygenase
    • Wolfe MD, Altier DJ, Stubna A, Popescu CV, Münck E, Lipscomb JD. (2002). Benzoate 1,2-dioxygenase from Pseudomonas putida: single turnover kinetics and regulation of a twocomponent Rieske dioxygenase. Biochemistry 41:9611-9626
    • (2002) Biochemistry , vol.41 , pp. 9611-9626
    • Wolfe, M.D.1    Altier, D.J.2    Stubna, A.3    Popescu, C.V.4    Münck, E.5    Lipscomb, J.D.6
  • 71
    • 33746460872 scopus 로고    scopus 로고
    • Neverland is an evolutionally conserved Rieske-domain protein that is essential for ecdysone synthesis and insect growth
    • Yoshiyama T, Namiki T, Mita K, Kataoka H, Niwa R. (2006). Neverland is an evolutionally conserved Rieske-domain protein that is essential for ecdysone synthesis and insect growth. Development 133:2565-2574
    • (2006) Development , vol.133 , pp. 2565-2574
    • Yoshiyama, T.1    Namiki, T.2    Mita, K.3    Kataoka, H.4    Niwa, R.5
  • 73
    • 0035434478 scopus 로고    scopus 로고
    • Multiple mutations at the active site of naphthalene dioxygenase affect regioselectivity and enantioselectivity
    • Yu CL, Parales RE, Gibson DT. (2001). Multiple mutations at the active site of naphthalene dioxygenase affect regioselectivity and enantioselectivity. J Ind Microbiol Biotechnol 27:94-103
    • (2001) J Ind Microbiol Biotechnol , vol.27 , pp. 94-103
    • Yu, C.L.1    Parales, R.E.2    Gibson, D.T.3


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