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Volumn 288, Issue 48, 2013, Pages 34767-34776

Structural basis of substrate conversion in a new aromatic peroxygenase: Cytochrome P450 functionality with benefits

Author keywords

[No Author keywords available]

Indexed keywords

ALIPHATIC HYDROCARBONS; CELLULAR ENVIRONMENT; LIGAND BINDING MODE; OXYFUNCTIONALIZATION; PEROXIDASE ACTIVITIES; SPATIAL RESTRICTIONS; SUBSTRATE CONVERSION; SUBSTRATE SPECIFICITY;

EID: 84889043335     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.514521     Document Type: Article
Times cited : (117)

References (51)
  • 1
    • 0000820085 scopus 로고
    • Selective intermolecular carbon- hydrogen bond activation by synthetic metal complexes in homogeneous solution
    • Arndtsen, B. A., Bergman, R. G., Mobley, T. A., and Peterson, T. H. (1995) Selective intermolecular carbon- hydrogen bond activation by synthetic metal complexes in homogeneous solution. Acc. Chem. Res. 28, 154 -162
    • (1995) Acc. Chem. Res , vol.28 , pp. 154-162
    • Arndtsen, B.A.1    Bergman, R.G.2    Mobley, T.A.3    Peterson, T.H.4
  • 3
    • 0242526099 scopus 로고    scopus 로고
    • Catalytic methods for C-H bond functionalization: Application in organic synthesis
    • Kakiuchi, F., and Chatani, N. (2003) Catalytic methods for C-H bond functionalization: application in organic synthesis. Adv. Synth. Catal. 345, 1077-1101
    • (2003) Adv. Synth. Catal , vol.345 , pp. 1077-1101
    • Kakiuchi, F.1    Chatani, N.2
  • 4
    • 84867570211 scopus 로고    scopus 로고
    • Catalytic, mild, and selective oxyfunctionalization of linear alkanes: Current challenges
    • Bordeaux, M., Galarneau, A., and Drone, J. (2012) Catalytic, mild, and selective oxyfunctionalization of linear alkanes: current challenges. Angew. Chem. Int. Ed. Engl. 51, 10712-10723
    • (2012) Angew. Chem. Int. Ed. Engl , vol.51 , pp. 10712-10723
    • Bordeaux, M.1    Galarneau, A.2    Drone, J.3
  • 5
    • 34249819058 scopus 로고    scopus 로고
    • Variations on a (t) heme - Novel mechanisms, redox partners and catalytic functions in the cytochrome P450 superfamily
    • Munro, A. W., Girvan, H. M., and McLean, K. J. (2007) Variations on a (t) heme - novel mechanisms, redox partners and catalytic functions in the cytochrome P450 superfamily. Nat. Prod. Rep. 24, 585-609
    • (2007) Nat. Prod. Rep , vol.24 , pp. 585-609
    • Munro, A.W.1    Girvan, H.M.2    McLean, K.J.3
  • 7
    • 0036560522 scopus 로고    scopus 로고
    • Cytochrome P450 enzymes in the generation of commercial products
    • Guengerich, F. P. (2002) Cytochrome P450 enzymes in the generation of commercial products. Nat. Rev. Drug Discov. 1, 359-366
    • (2002) Nat. Rev. Drug Discov , vol.1 , pp. 359-366
    • Guengerich, F.P.1
  • 8
    • 84861868170 scopus 로고    scopus 로고
    • Practical application of cytochrome P450
    • Sakaki, T. (2012) Practical application of cytochrome P450. Biol. Pharm. Bull. 35, 844-849
    • (2012) Biol. Pharm. Bull , vol.35 , pp. 844-849
    • Sakaki, T.1
  • 9
    • 33846979487 scopus 로고    scopus 로고
    • Enzymatic hydroxylation of aromatic compounds
    • Ullrich, R., and 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
  • 11
    • 4143095883 scopus 로고    scopus 로고
    • Novel haloperoxidase from the agaric basidiomycete Agrocybe aegerita oxidizes aryl alcohols and aldehydes
    • Ullrich, R., Nüske, J., Scheibner, K., Spantzel, J., and Hofrichter, M. (2004) Novel haloperoxidase from the agaric basidiomycete Agrocybe aegerita oxidizes aryl alcohols and aldehydes. Appl. Environ. Microbiol. 70, 4575- 4581
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 4575-4581
    • Ullrich, R.1    Nüske, J.2    Scheibner, K.3    Spantzel, J.4    Hofrichter, M.5
  • 12
    • 80052960977 scopus 로고    scopus 로고
    • Selective hydroxylation of alkanes by an extracellular fungal peroxygenase
    • Peter, S., Kinne, M., Wang, X., Ullrich, R., Kayser, G., Groves, J. T., and Hofrichter, M. (2011) Selective hydroxylation of alkanes by an extracellular fungal peroxygenase. FEBS J. 278, 3667-3675
    • (2011) FEBS J. , vol.278 , pp. 3667-3675
    • Peter, S.1    Kinne, M.2    Wang, X.3    Ullrich, R.4    Kayser, G.5    Groves, J.T.6    Hofrichter, M.7
  • 14
    • 80052745488 scopus 로고    scopus 로고
    • Regioselective oxygenation of fatty acids fatty alcohols and other aliphatic compounds by a basidiomycete heme-thiolate peroxidase
    • Gutiérrez, A., Babot, E. D., Ullrich, R., Hofrichter, M., Martínez, A. T., and del Río, J. C. (2011) Regioselective oxygenation of fatty acids, fatty alcohols and other aliphatic compounds by a basidiomycete heme-thiolate peroxidase. Arch. Biochem. Biophys. 514, 33-43
    • (2011) Arch Biochem Biophys , vol.514 , pp. 33-43
    • Gutiérrez, A.1    Babot, E.D.2    Ullrich, R.3    Hofrichter, M.4    Martínez, A.T.5    Del Río, J.C.6
  • 17
    • 0036605098 scopus 로고    scopus 로고
    • Polycyclic aromatic hydrocarbons: Environmental pollution and bioremediation
    • Samanta, S. K., Singh, O. V., and Jain, R. K. (2002) Polycyclic aromatic hydrocarbons: environmental pollution and bioremediation. Trends Biotechnol. 20, 243-248
    • (2002) Trends Biotechnol , vol.20 , pp. 243-248
    • Samanta, S.K.1    Singh, O.V.2    Jain, R.K.3
  • 18
    • 0019074870 scopus 로고
    • Benzo[a]pyrene metabolism, activation, and carcinogenesis: Role and regulation of mixed-function oxidases and related enzymes
    • Gelboin, H. V. (1980) Benzo[a]pyrene metabolism, activation, and carcinogenesis: role and regulation of mixed-function oxidases and related enzymes. Physiol. Rev. 60, 1107-1166
    • (1980) Physiol. Rev , vol.60 , pp. 1107-1166
    • Gelboin, H.V.1
  • 19
    • 0032959536 scopus 로고    scopus 로고
    • Formation of bound residues during microbial degradation of [14C]anthracene in soil
    • Kästner, M., Streibich, S., Beyrer, M., Richnow, H. H., and Fritsche, W. (1999) Formation of bound residues during microbial degradation of [14C]anthracene in soil. Appl. Environ. Microbiol. 65, 1834-1842
    • (1999) Appl. Environ. Microbiol , vol.65 , pp. 1834-1842
    • Kästner, M.1    Streibich, S.2    Beyrer, M.3    Richnow, H.H.4    Fritsche, W.5
  • 21
    • 0029646104 scopus 로고
    • The crystal structure of chloroperoxidase: A heme peroxidase-cytochrome P450 functional hybrid
    • Sundaramoorthy, M., Terner, J., and Poulos, T. L. (1995) The crystal structure of chloroperoxidase: a heme peroxidase-cytochrome P450 functional hybrid. Structure 3, 1367-1377
    • (1995) Structure , vol.3 , pp. 1367-1377
    • Sundaramoorthy, M.1    Terner, J.2    Poulos, T.L.3
  • 22
    • 33747732175 scopus 로고    scopus 로고
    • Crystal structures of chloroperoxidase with its bound substrates and complexed with formate, acetate, and nitrate
    • Kühnel, K., Blankenfeldt, W., Terner, J., and Schlichting, I. (2006) Crystal structures of chloroperoxidase with its bound substrates and complexed with formate, acetate, and nitrate. J. Biol. Chem. 281, 23990-23998
    • (2006) J. Biol. Chem , vol.281 , pp. 23990-23998
    • Kühnel, K.1    Blankenfeldt, W.2    Terner, J.3    Schlichting, I.4
  • 23
    • 77953151732 scopus 로고    scopus 로고
    • Crystallization of a 45 kDa peroxygenase/peroxidase from the mushroom Agrocybe aegerita and structure determination by SAD utilizing only the haem iron
    • Piontek, K., Ullrich, R., Liers, C., Diederichs, K., Plattner, D. A., and Hofrichter, M. (2010) Crystallization of a 45 kDa peroxygenase/peroxidase from the mushroom Agrocybe aegerita and structure determination by SAD utilizing only the haem iron. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66, 693-698
    • (2010) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun , vol.66 , pp. 693-698
    • Piontek, K.1    Ullrich, R.2    Liers, C.3    Diederichs, K.4    Plattner, D.A.5    Hofrichter, M.6
  • 24
    • 38349083847 scopus 로고    scopus 로고
    • Toxicity and carcinogenicity studies of 4-methylimidazole in F344/N rats and B6C3F1 mice
    • Chan, P. C., Hill, G. D., Kissling, G. E., and Nyska, A. (2008) Toxicity and carcinogenicity studies of 4-methylimidazole in F344/N rats and B6C3F1 mice. Arch. Toxicol. 82, 45-53
    • (2008) Arch. Toxicol , vol.82 , pp. 45-53
    • Chan, P.C.1    Hill, G.D.2    Kissling, G.E.3    Nyska, A.4
  • 26
    • 76449106188 scopus 로고    scopus 로고
    • Integration, scaling, space-group assignment and postrefinement
    • Kabsch, W. (2010) Integration, scaling, space-group assignment and postrefinement. Acta Crystallogr. D Biol. Crystallogr. 66, 133-144
    • (2010) Acta Crystallogr. D Biol. Crystallogr , vol.66 , pp. 133-144
    • Kabsch, W.1
  • 28
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • Sheldrick, G. M. (2008) A short history of SHELX. Acta Crystallogr. A 64, 112-122
    • (2008) Acta Crystallogr. A , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 30
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F1 ATPase
    • Abrahams, J. P., and Leslie, A. G. W. (1996) Methods used in the structure determination of bovine mitochondrial F1 ATPase. Acta Crystallogr. D Biol. Crystallogr. 52, 30-42
    • (1996) Acta Crystallogr. D Biol. Crystallogr , vol.52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.G.W.2
  • 31
    • 33748337934 scopus 로고    scopus 로고
    • The Buccaneer software for automated model building. 1. Tracing protein chains
    • Cowtan, K. (2006) The Buccaneer software for automated model building. 1. Tracing protein chains. Acta Crystallogr. D Biol. Crystallogr. 62, 1002-1011
    • (2006) Acta Crystallogr. D Biol. Crystallogr , vol.62 , pp. 1002-1011
    • Cowtan, K.1
  • 32
    • 13844301139 scopus 로고    scopus 로고
    • Direct incorporation of experimental phase information in model refinement
    • Skubák, P., Murshudov, G. N., and Pannu, N. S. (2004) Direct incorporation of experimental phase information in model refinement. Acta Crystallogr. D Biol. Crystallogr. 60, 2196-2201
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60 , pp. 2196-2201
    • Skubák, P.1    Murshudov, G.N.2    Pannu, N.S.3
  • 33
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P., and Cowtan, K. (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60, 2126-2132
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 36
    • 57649229060 scopus 로고    scopus 로고
    • HOLLOW: Generating accurate representations of channel and interior surfaces in molecular structures
    • Ho, B. K., and Gruswitz, F. (2008) HOLLOW: generating accurate representations of channel and interior surfaces in molecular structures. BMC Struct. Biol. 8, 49
    • (2008) BMC Struct. Biol , vol.8 , pp. 49
    • Ho, B.K.1    Gruswitz, F.2
  • 37
    • 33744826819 scopus 로고    scopus 로고
    • MolDock: A new technique for high-accuracy molecular docking
    • Thomsen, R., and Christensen, M. H. (2006) MolDock: a new technique for high-accuracy molecular docking. J. Med. Chem. 49, 3315-3321
    • (2006) J. Med. Chem , vol.49 , pp. 3315-3321
    • Thomsen, R.1    Christensen, M.H.2
  • 38
    • 0037044587 scopus 로고    scopus 로고
    • Gas chromatographic-mass spectrometric quantification of 4-(5-)-methylimidazole in roasted coffee after ion-pair extraction
    • Casal, S., Fernandes, J. O., Oliveira, M. B. P. P., and Ferreira, M. A. (2002) Gas chromatographic-mass spectrometric quantification of 4-(5-)-methylimidazole in roasted coffee after ion-pair extraction. J. Chromatogr. A 976, 285-291
    • (2002) J. Chromatogr. A , vol.976 , pp. 285-291
    • Casal, S.1    Fernandes, J.O.2    Oliveira, M.B.P.P.3    Ferreira, M.A.4
  • 40
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld, R., and Kornfeld, S. (1985) Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 54, 631-664
    • (1985) Annu. Rev. Biochem , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 41
    • 84864668830 scopus 로고    scopus 로고
    • Detection and kinetic characterization of a highly reactive heme-thiolate peroxygenase Compound i
    • Wang, X., Peter, S., Kinne, M., Hofrichter, M., and Groves, J. T. (2012) Detection and kinetic characterization of a highly reactive heme-thiolate peroxygenase Compound I. J. Am. Chem. Soc. 134, 12897-12900
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 12897-12900
    • Wang, X.1    Peter, S.2    Kinne, M.3    Hofrichter, M.4    Groves, J.T.5
  • 42
    • 0028587337 scopus 로고
    • The crystal structure of manganese peroxidase from Phanerochaete chrysosporium at 2.06-Å resolution
    • Sundaramoorthy, M., Kishi, K., Gold, M. H., and Poulos, T. L. (1994) The crystal structure of manganese peroxidase from Phanerochaete chrysosporium at 2.06-Å resolution. J. Biol. Chem. 269, 32759-32767
    • (1994) J. Biol. Chem , vol.269 , pp. 32759-32767
    • Sundaramoorthy, M.1    Kishi, K.2    Gold, M.H.3    Poulos, T.L.4
  • 43
    • 0022502712 scopus 로고
    • Ligand and halide binding properties of chloroperoxidase: Peroxidase-type active site heme environment with cytochrome P-450 type endogenous axial ligand and spectroscopic properties
    • Sono, M., Dawson, J. H., Hall, K., and Hager, L. P. (1986) Ligand and halide binding properties of chloroperoxidase: peroxidase-type active site heme environment with cytochrome P-450 type endogenous axial ligand and spectroscopic properties. Biochemistry 25, 347-356
    • (1986) Biochemistry , vol.25 , pp. 347-356
    • Sono, M.1    Dawson, J.H.2    Hall, K.3    Hager, L.P.4
  • 45
    • 77950459712 scopus 로고    scopus 로고
    • Conversion of polycyclic aromatic hydrocarbons, methyl naphthalenes and dibenzofuran by two fungal peroxygenases
    • Aranda, E., Ullrich, R., and Hofrichter, M. (2010) Conversion of polycyclic aromatic hydrocarbons, methyl naphthalenes and dibenzofuran by two fungal peroxygenases. Biodegradation 21, 267-281
    • (2010) Biodegradation , vol.21 , pp. 267-281
    • Aranda, E.1    Ullrich, R.2    Hofrichter, M.3
  • 46
    • 78751520949 scopus 로고    scopus 로고
    • Formation of carcinogenic 4(5)- methylimidazole in Maillard reaction systems
    • Moon, J.-K., and Shibamoto, T. (2011) Formation of carcinogenic 4(5)- methylimidazole in Maillard reaction systems. J. Agric. Food. Chem. 59, 615-618
    • (2011) J Agric Food Chem , vol.59 , pp. 615-618
    • Moon, J.-K.1    Shibamoto, T.2
  • 47
    • 33750370837 scopus 로고    scopus 로고
    • Cytochrome P450 active site plasticity: Attenuation of imidazole binding in cytochrome P450cam by an L244A mutation
    • Verras, A., Alian, A., and Ortiz de Montellano, P. R. (2006) Cytochrome P450 active site plasticity: attenuation of imidazole binding in cytochrome P450cam by an L244A mutation. Protein Eng. Des. Sel. 19, 491-496
    • (2006) Protein Eng. Des. Sel , vol.19 , pp. 491-496
    • Verras, A.1    Alian, A.2    Ortiz De Montellano, P.R.3
  • 48
    • 0019321508 scopus 로고
    • The stereochemistry of peroxidase catalysis
    • Poulos, T. L., and Kraut, J. (1980) The stereochemistry of peroxidase catalysis. J. Biol. Chem. 255, 8199-8205
    • (1980) J. Biol. Chem , vol.255 , pp. 8199-8205
    • Poulos, T.L.1    Kraut, J.2
  • 49
    • 84873638013 scopus 로고    scopus 로고
    • First crystal structure of a fungal high-redox potential dye-decolorizing peroxidase. Substrate interaction sites and long-range electron transfer
    • Strittmatter, E., Liers, C., Ullrich, R., Wachter, S., Hofrichter, M., Plattner, D. A., and Piontek, K. (2013) First crystal structure of a fungal high-redox potential dye-decolorizing peroxidase. Substrate interaction sites and long-range electron transfer. J. Biol. Chem. 288, 4095- 4102
    • (2013) J. Biol. Chem , vol.288 , pp. 4095-4102
    • Strittmatter, E.1    Liers, C.2    Ullrich, R.3    Wachter, S.4    Hofrichter, M.5    Plattner, D.A.6    Piontek, K.7
  • 51
    • 0033605084 scopus 로고    scopus 로고
    • The crystal structure of lignin peroxidase at 1.70 Å resolution reveals a hydroxy group on the C of tryptophan 171: A novel radical site formed during the redox cycle
    • Choinowski, T., Blodig, W., Winterhalter, K. H., and Piontek, K. (1999) The crystal structure of lignin peroxidase at 1.70 Å resolution reveals a hydroxy group on the C of tryptophan 171: a novel radical site formed during the redox cycle. J. Mol. Biol. 286, 809-827
    • (1999) J. Mol. Biol , vol.286 , pp. 809-827
    • Choinowski, T.1    Blodig, W.2    Winterhalter, K.H.3    Piontek, K.4


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