메뉴 건너뛰기




Volumn 117, Issue 28, 2013, Pages 8301-8309

Kinetic study of the inhibition mechanism of dehaloperoxidase-hemoglobin a by 4-bromophenol

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; HEMOGLOBIN; REACTION INTERMEDIATES; SINGULAR VALUE DECOMPOSITION;

EID: 84880547280     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp3116353     Document Type: Article
Times cited : (19)

References (44)
  • 1
    • 0039316844 scopus 로고    scopus 로고
    • An Unusual Dehalogenating Peroxidase from the Marine Terebellid Polychaete Amphitrite ornata
    • Chen, Y. P.; Woodin, S. A.; Lincoln, D. E.; Lovell, C. R. An Unusual Dehalogenating Peroxidase from the Marine Terebellid Polychaete Amphitrite ornata J. Biol. Chem. 1996, 271, 4609-12
    • (1996) J. Biol. Chem. , vol.271 , pp. 4609-4612
    • Chen, Y.P.1    Woodin, S.A.2    Lincoln, D.E.3    Lovell, C.R.4
  • 5
    • 84857680632 scopus 로고    scopus 로고
    • Optimization of Operational Conditions for Biodegradation of Chlorophenols by Laccase-polyacrilonitrile Beads System
    • Menale, C.; Nicolucci, C.; Catapane, M.; Rossi, S.; Bencivenga, U.; Mita, D. G.; Diano, N. Optimization of Operational Conditions for Biodegradation of Chlorophenols by Laccase-polyacrilonitrile Beads System J. Mol. Catal. B-Enzym. 2012, 78, 38-44
    • (2012) J. Mol. Catal. B-Enzym. , vol.78 , pp. 38-44
    • Menale, C.1    Nicolucci, C.2    Catapane, M.3    Rossi, S.4    Bencivenga, U.5    Mita, D.G.6    Diano, N.7
  • 6
    • 33846029162 scopus 로고    scopus 로고
    • The pH Dependence of the Activity of Dehaloperoxidase from Amphitrite ornata
    • Franzen, S.; Gilvey, L. B.; Belyea, J. L. The pH Dependence of the Activity of Dehaloperoxidase from Amphitrite ornata Biochim. Biophys. Acta-Prot. Proteom. 2007, 1774, 121-130
    • (2007) Biochim. Biophys. Acta-Prot. Proteom. , vol.1774 , pp. 121-130
    • Franzen, S.1    Gilvey, L.B.2    Belyea, J.L.3
  • 7
    • 64349114283 scopus 로고    scopus 로고
    • Different Modes of Binding of Mono-, Di-, and Trihalogenated Phenols to the Hemoglobin Dehaloperoxidase from Amphitrite ornata
    • Davis, M. F.; Gracz, H.; Vendeix, F. A. P.; de Serrano, V.; Somasundaram, A.; Decatur, S. M.; Franzen, S. Different Modes of Binding of Mono-, Di-, and Trihalogenated Phenols to the Hemoglobin Dehaloperoxidase from Amphitrite ornata Biochemistry 2009, 48, 2164-2172
    • (2009) Biochemistry , vol.48 , pp. 2164-2172
    • Davis, M.F.1    Gracz, H.2    Vendeix, F.A.P.3    De Serrano, V.4    Somasundaram, A.5    Decatur, S.M.6    Franzen, S.7
  • 9
  • 10
  • 13
    • 16844363189 scopus 로고    scopus 로고
    • Bromophenol Accumulation and Sediment Contamination by the Marine Annelids Notomastus lobatus and Thelepus crispus
    • Lincoln, D. E.; Fielman, K. T.; Marinelli, R. L.; Woodin, S. A. Bromophenol Accumulation and Sediment Contamination by the Marine Annelids Notomastus lobatus and Thelepus crispus Biochem. System. Ecol. 2005, 33, 559-570
    • (2005) Biochem. System. Ecol. , vol.33 , pp. 559-570
    • Lincoln, D.E.1    Fielman, K.T.2    Marinelli, R.L.3    Woodin, S.A.4
  • 14
    • 84875793959 scopus 로고    scopus 로고
    • Structural Evidence for Stabilization of Inhibitor Binding by a Protein Cavity in the Dehaloperoxidase-hemoglobin from Amphitrite ornata
    • de Serrano, V.; Franzen, S. Structural Evidence for Stabilization of Inhibitor Binding by a Protein Cavity in the Dehaloperoxidase-hemoglobin from Amphitrite ornata Pept. Sci. 2012, 98, 27-35
    • (2012) Pept. Sci. , vol.98 , pp. 27-35
    • De Serrano, V.1    Franzen, S.2
  • 15
    • 77958479015 scopus 로고    scopus 로고
    • Probing the Oxyferrous and Catalytically Active Ferryl States of Amphitrite ornata Dehaloperoxidase by Cryoreduction and EPR/ENDOR Spectroscopy. Detection of Compound i
    • Davydov, R.; Osborne, R. L.; Shanmugam, M.; Du, J.; Dawson, J. H.; Hoffman, B. M. Probing the Oxyferrous and Catalytically Active Ferryl States of Amphitrite ornata Dehaloperoxidase by Cryoreduction and EPR/ENDOR Spectroscopy. Detection of Compound I J. Am. Chem. Soc. 2010, 132, 14995-15004
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 14995-15004
    • Davydov, R.1    Osborne, R.L.2    Shanmugam, M.3    Du, J.4    Dawson, J.H.5    Hoffman, B.M.6
  • 16
    • 34548209135 scopus 로고    scopus 로고
    • 2-Dependent Oxidative Dehalogenation of Chlorophenols to DNA-Binding Radicals and Quinones
    • 2-Dependent Oxidative Dehalogenation of Chlorophenols to DNA-Binding Radicals and Quinones Biochemistry 2007, 46, 9823-9829
    • (2007) Biochemistry , vol.46 , pp. 9823-9829
    • Osborne, R.L.1    Coggins, M.K.2    Walla, M.3    Dawson, J.H.4
  • 17
    • 28544440508 scopus 로고    scopus 로고
    • Enzyme Function of the Globin Dehaloperoxidase from Amphitrite ornata Is Activated by Substrate Binding
    • Belyea, J.; Gilvey, L. B.; Davis, M. F.; Godek, M.; Sit, T. L.; Lommel, S. A.; Franzen, S. Enzyme Function of the Globin Dehaloperoxidase from Amphitrite ornata Is Activated by Substrate Binding Biochemistry 2005, 44, 15637-15644
    • (2005) Biochemistry , vol.44 , pp. 15637-15644
    • Belyea, J.1    Gilvey, L.B.2    Davis, M.F.3    Godek, M.4    Sit, T.L.5    Lommel, S.A.6    Franzen, S.7
  • 18
    • 78549237806 scopus 로고    scopus 로고
    • Kinetic Analysis of a Naturally Occurring Bioremediation Enzyme: Dehaloperoxidase-hemoglobin from Amphitrite ornata
    • Ma, H.; Thompson, M. K.; Gaff, J.; Franzen, S. Kinetic Analysis of a Naturally Occurring Bioremediation Enzyme: Dehaloperoxidase-hemoglobin from Amphitrite ornata J. Phys. Chem. B 2010, 114, 13823-9
    • (2010) J. Phys. Chem. B , vol.114 , pp. 13823-13829
    • Ma, H.1    Thompson, M.K.2    Gaff, J.3    Franzen, S.4
  • 19
    • 3042734504 scopus 로고    scopus 로고
    • Crystal Structure of the Ascorbate Peroxidase-Salicylhydroxamic Acid Complex
    • Sharp, K. H.; Moody, P. C. E.; Brown, K. A.; Raven, E. L. Crystal Structure of the Ascorbate Peroxidase-Salicylhydroxamic Acid Complex Biochemistry 2004, 43, 8644-8651
    • (2004) Biochemistry , vol.43 , pp. 8644-8651
    • Sharp, K.H.1    Moody, P.C.E.2    Brown, K.A.3    Raven, E.L.4
  • 20
    • 76749095979 scopus 로고    scopus 로고
    • Determination of Separate Inhibitor and Substrate Binding Sites in the Dehaloperoxidase-Hemoglobin from Amphitrite ornata
    • Davis, M. F.; Bobay, B. G.; Franzen, S. Determination of Separate Inhibitor and Substrate Binding Sites in the Dehaloperoxidase-Hemoglobin from Amphitrite ornata Biochemistry 2010, 49, 1199-1206
    • (2010) Biochemistry , vol.49 , pp. 1199-1206
    • Davis, M.F.1    Bobay, B.G.2    Franzen, S.3
  • 21
    • 84875986002 scopus 로고    scopus 로고
    • Structural and Kinetic Study of an Internal Substrate Binding Site in Dehaloperoxidase-Hemoglobin A from Amphitrite ornata
    • Zhao, J.; de Serrano, V.; Zhao, J.; Le, P.; Franzen, S. Structural and Kinetic Study of an Internal Substrate Binding Site in Dehaloperoxidase- Hemoglobin A from Amphitrite ornata Biochemistry 2013, 52, 2427-2439
    • (2013) Biochemistry , vol.52 , pp. 2427-2439
    • Zhao, J.1    De Serrano, V.2    Zhao, J.3    Le, P.4    Franzen, S.5
  • 22
    • 79959950550 scopus 로고    scopus 로고
    • Reactivity of Deoxy- and Oxyferrous Dehaloperoxidase B from Amphitrite ornata: Identification of Compound II and Its Ferrous-Hydroperoxide Precursor
    • D'Antonio, J.; Ghiladi, R. A. Reactivity of Deoxy- and Oxyferrous Dehaloperoxidase B from Amphitrite ornata: Identification of Compound II and Its Ferrous-Hydroperoxide Precursor Biochemistry 2011, 50, 5999-6011
    • (2011) Biochemistry , vol.50 , pp. 5999-6011
    • D'Antonio, J.1    Ghiladi, R.A.2
  • 23
    • 0037044754 scopus 로고    scopus 로고
    • Formation and Decay of Hydroperoxo-Ferric Heme Complex in Horseradish Peroxidase studied by Cryoradiolysis
    • Denisov, I. G.; Makris, T. M.; Sligar, S. G. Formation and Decay of Hydroperoxo-Ferric Heme Complex in Horseradish Peroxidase studied by Cryoradiolysis J. Biol. Chem. 2002, 277, 42706-42710
    • (2002) J. Biol. Chem. , vol.277 , pp. 42706-42710
    • Denisov, I.G.1    Makris, T.M.2    Sligar, S.G.3
  • 24
    • 0028978228 scopus 로고
    • Horseradish Peroxidase Phe(172)- Tyr Mutant - Sequential Formation of Compound-I with a Porphyrin Cation and a Protein Radical
    • Miller, V. P.; Goodin, D. B.; Friedman, A. E.; Hartmann, C.; Demontellano, P. R. O. Horseradish Peroxidase Phe(172)- Tyr Mutant-Sequential Formation of Compound-I with a Porphyrin Cation and a Protein Radical J. Biol. Chem. 1995, 270, 18413-18419
    • (1995) J. Biol. Chem. , vol.270 , pp. 18413-18419
    • Miller, V.P.1    Goodin, D.B.2    Friedman, A.E.3    Hartmann, C.4    Demontellano, P.R.O.5
  • 25
    • 85067719821 scopus 로고
    • Identification by ENDOR of Trp191 as the Free-Radical Site in Cytochrome c Peroxidase Compound ES
    • Aisen, P. Identification by ENDOR of Trp191 as the Free-Radical Site in Cytochrome c Peroxidase Compound ES Chemtracts: Biochem. Mol. Biol. 1990, 1, 441-3
    • (1990) Chemtracts: Biochem. Mol. Biol. , vol.1 , pp. 441-443
    • Aisen, P.1
  • 26
    • 1642503542 scopus 로고
    • Studies of the Radical Species in Compound ES of Cytochrome c Peroxidase Altered by Site-Directed Mutagenesis
    • Goodin, D. B.; Mauk, A. G.; Smith, M. Studies of the Radical Species in Compound ES of Cytochrome c Peroxidase Altered by Site-Directed Mutagenesis Proc. Natl. Acad. Sci. U. S. A. 1986, 83, 1295-1299
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 1295-1299
    • Goodin, D.B.1    Mauk, A.G.2    Smith, M.3
  • 27
    • 61449121236 scopus 로고    scopus 로고
    • Characterization of Dehaloperoxidase Compound ES and Its Reactivity with Trihalophenols
    • Feducia, J.; Dumarieh, R.; Gilvey, L. B. G.; Smirnova, T.; Franzen, S.; Ghiladi, R. A. Characterization of Dehaloperoxidase Compound ES and Its Reactivity with Trihalophenols Biochemistry 2009, 48, 995-1005
    • (2009) Biochemistry , vol.48 , pp. 995-1005
    • Feducia, J.1    Dumarieh, R.2    Gilvey, L.B.G.3    Smirnova, T.4    Franzen, S.5    Ghiladi, R.A.6
  • 28
    • 78650119268 scopus 로고    scopus 로고
    • Compound ES of Dehaloperoxidase Decays via Two Alternative Pathways Depending on the Conformation of the Distal Histidine
    • Thompson, M. K.; Franzen, S.; Ghiladi, R. A.; Reeder, B. J.; Svistunenko, D. A. Compound ES of Dehaloperoxidase Decays via Two Alternative Pathways Depending on the Conformation of the Distal Histidine J. Am. Chem. Soc. 2010, 132, 17501-17510
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 17501-17510
    • Thompson, M.K.1    Franzen, S.2    Ghiladi, R.A.3    Reeder, B.J.4    Svistunenko, D.A.5
  • 30
    • 0028021633 scopus 로고
    • Time-Resolved Optical Absorption Studies of Intramolecular Electron Transfer in Cytochrome c Oxidase
    • Georgiadis, K. E.; Jhon, N.-I.; Einarsdottir, O. Time-Resolved Optical Absorption Studies of Intramolecular Electron Transfer in Cytochrome c Oxidase Biochemistry 1994, 33, 9245-9256
    • (1994) Biochemistry , vol.33 , pp. 9245-9256
    • Georgiadis, K.E.1    Jhon, N.-I.2    Einarsdottir, O.3
  • 31
    • 77951003275 scopus 로고    scopus 로고
    • Cytochrome P450: The Active Oxidant and Its Spectrum
    • Rittle, J.; Younker, J. M.; Green, M. T. Cytochrome P450: The Active Oxidant and Its Spectrum Inorg. Chem. 2010, 49, 3610-3617
    • (2010) Inorg. Chem. , vol.49 , pp. 3610-3617
    • Rittle, J.1    Younker, J.M.2    Green, M.T.3
  • 32
    • 33746584767 scopus 로고    scopus 로고
    • Proximal Cavity, Distal Histidine, and Substrate Hydrogen-Bonding Mutations Modulate the Activity of Amphitrite ornata Dehaloperoxidase
    • Franzen, S.; Belyea, J.; Gilvey, L. B.; Davis, M. F.; Chaudhary, C. E.; Sit, T. L.; Lommel, S. A. Proximal Cavity, Distal Histidine, and Substrate Hydrogen-Bonding Mutations Modulate the Activity of Amphitrite ornata Dehaloperoxidase Biochemistry 2006, 45, 9085-9094
    • (2006) Biochemistry , vol.45 , pp. 9085-9094
    • Franzen, S.1    Belyea, J.2    Gilvey, L.B.3    Davis, M.F.4    Chaudhary, C.E.5    Sit, T.L.6    Lommel, S.A.7
  • 35
    • 0029986887 scopus 로고    scopus 로고
    • Crystal structures of CO-, deoxy- and Met-Myoglobins at Various pH Values
    • Yang, F.; Phillips, G. N., Jr. Crystal structures of CO-, deoxy- and Met-Myoglobins at Various pH Values J. Mol. Biol. 1996, 256, 762-774
    • (1996) J. Mol. Biol. , vol.256 , pp. 762-774
    • Yang, F.1    Phillips, Jr.G.N.2
  • 36
    • 78650626762 scopus 로고    scopus 로고
    • Thermochemistry of Proton-Coupled Electron Transfer Reagents and its Implications
    • Warren, J. J.; Tronic, T. A.; Mayer, J. M. Thermochemistry of Proton-Coupled Electron Transfer Reagents and its Implications Chem. Rev. 2010, 110, 6961-7001
    • (2010) Chem. Rev. , vol.110 , pp. 6961-7001
    • Warren, J.J.1    Tronic, T.A.2    Mayer, J.M.3
  • 37
  • 38
    • 77954310525 scopus 로고    scopus 로고
    • AnAanalysis of Substrate Binding Interactions in the Heme Peroxidase Enzymes: A Structural Perspective
    • Gumiero, A.; Murphy, E. J.; Metcalfe, C. L.; Moody, P. C. E.; Raven, E. L. AnAanalysis of Substrate Binding Interactions in the Heme Peroxidase Enzymes: A Structural Perspective Arch. Biochem. Biophys. 2010, 13-20
    • (2010) Arch. Biochem. Biophys. , pp. 13-20
    • Gumiero, A.1    Murphy, E.J.2    Metcalfe, C.L.3    Moody, P.C.E.4    Raven, E.L.5
  • 39
    • 34748844557 scopus 로고    scopus 로고
    • X-ray Crystal Structural Analysis of the Binding Site in the Ferric and Oxyferrous Forms of the Recombinant Heme Dehaloperoxidase Cloned from Amphitrite ornata
    • de Serrano, V.; Chen, Z. X.; Davis, M. F.; Franzen, S. X-ray Crystal Structural Analysis of the Binding Site in the Ferric and Oxyferrous Forms of the Recombinant Heme Dehaloperoxidase Cloned from Amphitrite ornata Acta Crystallogr., Sect.D: Biol. Crystal. 2007, 63, 1094-1101
    • (2007) Acta Crystallogr., Sect.D: Biol. Crystal. , vol.63 , pp. 1094-1101
    • De Serrano, V.1    Chen, Z.X.2    Davis, M.F.3    Franzen, S.4
  • 41
    • 0033580622 scopus 로고    scopus 로고
    • Widespread Occurrence of Natural Halogenated Organics among Temperate Marine Infauna
    • Fielman, K. T.; Woodin, S. A.; Walla, M. D.; Lincoln, D. E. Widespread Occurrence of Natural Halogenated Organics among Temperate Marine Infauna Marine Ecol.-Prog. Ser. 1999, 181, 1-12
    • (1999) Marine Ecol.-Prog. Ser. , vol.181 , pp. 1-12
    • Fielman, K.T.1    Woodin, S.A.2    Walla, M.D.3    Lincoln, D.E.4
  • 42
    • 0033560939 scopus 로고    scopus 로고
    • Activity of Marine Sediment Bacterial Communities Exposed to 4-bromophenol, a Polychaete Secondary Metabolite
    • Lovell, C. R.; Steward, C. C.; Phillips, T. Activity of Marine Sediment Bacterial Communities Exposed to 4-bromophenol, a Polychaete Secondary Metabolite Marine Ecol.-Prog. Ser. 1999, 179, 241-246
    • (1999) Marine Ecol.-Prog. Ser. , vol.179 , pp. 241-246
    • Lovell, C.R.1    Steward, C.C.2    Phillips, T.3
  • 43
    • 81755172331 scopus 로고    scopus 로고
    • Revisiting the Peroxidase Oxidation of 2,4,6-Trihalophenols: ESR Detection of Radical Intermediates
    • Sturgeon, B. E.; Battenburg, B. J.; Lyon, B. J.; Franzen, S. Revisiting the Peroxidase Oxidation of 2,4,6-Trihalophenols: ESR Detection of Radical Intermediates Chem. Res. Toxicol. 2011, 24, 1862-1868
    • (2011) Chem. Res. Toxicol. , vol.24 , pp. 1862-1868
    • Sturgeon, B.E.1    Battenburg, B.J.2    Lyon, B.J.3    Franzen, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.