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Volumn 53, Issue 44, 2014, Pages 6863-6877

Correlation of heme binding affinity and enzyme kinetics of dehaloperoxidase

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING ENERGY; CHEMICAL STABILITY; DENATURATION; DIFFERENTIAL SCANNING CALORIMETRY; DRUG PRODUCTS; EFFICIENCY; ENZYME KINETICS; EXPERIMENTS; METABOLISM; ULTRAVIOLET VISIBLE SPECTROSCOPY; UREA;

EID: 84909592169     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi5005975     Document Type: Article
Times cited : (18)

References (84)
  • 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., and Lovell, C. R. (1996) An unusual dehalogenating peroxidase from the marine terebellid polychaete Amphitrite ornata J. Biol. Chem. 271, 4609-4612
    • (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
  • 2
    • 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. and Ghiladi, R. A. (2011) Reactivity of Deoxy- and Oxyferrous Dehaloperoxidase B from Amphitrite ornata: Identification of Compound II and Its Ferrous-Hydroperoxide Precursor Biochemistry 50, 5999-6011
    • (2011) Biochemistry , vol.50 , pp. 5999-6011
    • D'Antonio, J.1    Ghiladi, R.A.2
  • 3
    • 0034794637 scopus 로고    scopus 로고
    • Amphitrite ornata, a marine worm, contains two dehaloperoxidase genes
    • Han, K., Woodin, S. A., Lincoln, D. E., Fielman, K. T., and Ely, B. (2001) Amphitrite ornata, a marine worm, contains two dehaloperoxidase genes Mar. Biotechnol. 3, 287-292
    • (2001) Mar. Biotechnol. , vol.3 , pp. 287-292
    • Han, K.1    Woodin, S.A.2    Lincoln, D.E.3    Fielman, K.T.4    Ely, B.5
  • 9
    • 0034705539 scopus 로고    scopus 로고
    • The crystal structure and amino acid sequence of dehaloperoxidase from Amphitrite ornata indicate common ancestry with globins
    • LaCount, M. W., Zhang, E., Chen, Y. P., Han, K., Whitton, M. M., Lincoln, D. E., Woodin, S. A., and Lebioda, L. (2000) The crystal structure and amino acid sequence of dehaloperoxidase from Amphitrite ornata indicate common ancestry with globins J. Biol. Chem. 275, 18712-18716
    • (2000) J. Biol. Chem. , vol.275 , pp. 18712-18716
    • Lacount, M.W.1    Zhang, E.2    Chen, Y.P.3    Han, K.4    Whitton, M.M.5    Lincoln, D.E.6    Woodin, S.A.7    Lebioda, L.8
  • 11
    • 77749259052 scopus 로고    scopus 로고
    • New insights into the role of distal histidine flexibility in ligand stabilization of dehaloperoxidase-hemoglobin from Amphitrite ornata
    • Nicoletti, F. P., Thompson, M. K., Howes, B. D., Franzen, S., and Smulevich, G. (2010) New insights into the role of distal histidine flexibility in ligand stabilization of dehaloperoxidase-hemoglobin from Amphitrite ornata Biochemistry 49, 1903-1912
    • (2010) Biochemistry , vol.49 , pp. 1903-1912
    • Nicoletti, F.P.1    Thompson, M.K.2    Howes, B.D.3    Franzen, S.4    Smulevich, G.5
  • 13
    • 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., and Franzen, S. (2010) Determination of Separate Inhibitor and Substrate Binding Sites in the Dehaloperoxidase-Hemoglobin from Amphitrite ornata Biochemistry 49, 1199-1206
    • (2010) Biochemistry , vol.49 , pp. 1199-1206
    • Davis, M.F.1    Bobay, B.G.2    Franzen, S.3
  • 14
    • 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., and Franzen, S. (2009) Different Modes of Binding of Mono-, Di-, and Trihalogenated Phenols to the Hemoglobin Dehaloperoxidase from Amphitrite ornata Biochemistry 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
  • 15
    • 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. J., Le, P., and Franzen, S. (2013) Structural and Kinetic Study of an Internal Substrate Binding Site in Dehaloperoxidase-Hemoglobin A from Amphitrite ornata Biochemistry 52, 2427-2439
    • (2013) Biochemistry , vol.52 , pp. 2427-2439
    • Zhao, J.1    De Serrano, V.2    Zhao, J.J.3    Le, P.4    Franzen, S.5
  • 16
    • 84884227847 scopus 로고    scopus 로고
    • Complexes of Dual-Function Hemoglobin/Dehaloperoxidase with Substrate 2,4,6-Trichlorophenol Are Inhibitory and Indicate Binding of Halophenol to Compound i
    • Wang, C., Lovelace, L. L., Sun, S., Dawson, J. H., and Lebioda, L. (2013) Complexes of Dual-Function Hemoglobin/Dehaloperoxidase with Substrate 2,4,6-Trichlorophenol Are Inhibitory and Indicate Binding of Halophenol to Compound I Biochemistry 52, 6203-6210
    • (2013) Biochemistry , vol.52 , pp. 6203-6210
    • Wang, C.1    Lovelace, L.L.2    Sun, S.3    Dawson, J.H.4    Lebioda, L.5
  • 17
    • 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., and Franzen, S. (2011) Revisiting the peroxidase oxidation of 2,4,6-trihalophenols: ESR detection of radical intermediates Chem. Res. Toxicol. 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
  • 18
    • 84872486657 scopus 로고    scopus 로고
    • Catalytic efficiency of dehaloperoxidase A is controlled by electrostatics: Application of the vibrational Stark effect to understand enzyme kinetics
    • Schkolnik, G., Utesch, T., Zhao, J. J., Jiang, S., Thompson, M. K., Mroginski, M. A., Hildebrandt, P., and Franzen, S. (2013) Catalytic efficiency of dehaloperoxidase A is controlled by electrostatics: Application of the vibrational Stark effect to understand enzyme kinetics Biochem. Biophys. Res. Commun. 430, 1011-1015
    • (2013) Biochem. Biophys. Res. Commun. , vol.430 , pp. 1011-1015
    • Schkolnik, G.1    Utesch, T.2    Zhao, J.J.3    Jiang, S.4    Thompson, M.K.5    Mroginski, M.A.6    Hildebrandt, P.7    Franzen, S.8
  • 20
    • 0023644531 scopus 로고
    • Protein control of prosthetic heme reactivity. Reaction of substrates with the heme edge of horseradish peroxidase
    • Ator, M. A. and Ortiz de Montellano, P. R. (1987) Protein control of prosthetic heme reactivity. Reaction of substrates with the heme edge of horseradish peroxidase J. Biol. Chem. 262, 1542-1551
    • (1987) J. Biol. Chem. , vol.262 , pp. 1542-1551
    • Ator, M.A.1    Ortiz De Montellano, P.R.2
  • 21
    • 0028065004 scopus 로고
    • Thermodynamic prediction of structural determinants of the molten globule state of barnase
    • Freire, E. and Xie, D. (1994) Thermodynamic prediction of structural determinants of the molten globule state of barnase Biophys. Chem. 51, 243-251
    • (1994) Biophys. Chem. , vol.51 , pp. 243-251
    • Freire, E.1    Xie, D.2
  • 22
    • 0033642945 scopus 로고    scopus 로고
    • Structural stability of binding sites: Consequences for binding affinity and allosteric effects
    • Luque, I. and Freire, E. (2000) Structural stability of binding sites: Consequences for binding affinity and allosteric effects Proteins Suppl. 4, 63-71
    • (2000) Proteins Suppl. , vol.4 , pp. 63-71
    • Luque, I.1    Freire, E.2
  • 23
    • 0029737827 scopus 로고    scopus 로고
    • The stability of holomyoglobin is determined by heme affinity
    • Hargrove, M. S. and Olson, J. S. (1996) The stability of holomyoglobin is determined by heme affinity Biochemistry 35, 11310-11318
    • (1996) Biochemistry , vol.35 , pp. 11310-11318
    • Hargrove, M.S.1    Olson, J.S.2
  • 25
    • 0029737668 scopus 로고    scopus 로고
    • Structural factors governing hemin dissociation from metmyoglobin
    • Hargrove, M. S., Wilkinson, A. J., and Olson, J. S. (1996) Structural factors governing hemin dissociation from metmyoglobin Biochemistry 35, 11300-11309
    • (1996) Biochemistry , vol.35 , pp. 11300-11309
    • Hargrove, M.S.1    Wilkinson, A.J.2    Olson, J.S.3
  • 26
    • 77952040623 scopus 로고    scopus 로고
    • Structure of dehaloperoxidase B at 1.58 angstrom resolution and structural characterization of the AB dimer from Amphitrite ornata
    • de Serrano, V., D'Antonio, J., Franzen, S., and Ghiladi, R. A. (2010) Structure of dehaloperoxidase B at 1.58 angstrom resolution and structural characterization of the AB dimer from Amphitrite ornata Acta Crystallogr. D66, 529-538
    • (2010) Acta Crystallogr. , vol.66 , pp. 529-538
    • De Serrano, V.1    D'Antonio, J.2    Franzen, S.3    Ghiladi, R.A.4
  • 28
    • 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. and Franzen, S. (2012) Structural evidence for stabilization of inhibitor binding by a protein cavity in the dehaloperoxidase-hemoglobin from Amphitrite ornata Pept. Sci. 98, 27-35
    • (2012) Pept. Sci. , vol.98 , pp. 27-35
    • De Serrano, V.1    Franzen, S.2
  • 29
    • 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., and Franzen, S. (2010) Kinetic analysis of a naturally occurring bioremediation enzyme: Dehaloperoxidase-hemoglobin from Amphitrite ornata J. Phys. Chem. B 114, 13823-13829
    • (2010) J. Phys. Chem. B , vol.114 , pp. 13823-13829
    • Ma, H.1    Thompson, M.K.2    Gaff, J.3    Franzen, S.4
  • 31
    • 49749199032 scopus 로고
    • Cleavage of the Haem-Protein Link by Acid Methylethylketone
    • Teale, F. W. J. (1959) Cleavage of the Haem-Protein Link by Acid Methylethylketone Biochim. Biophys. Acta 35, 543
    • (1959) Biochim. Biophys. Acta , vol.35 , pp. 543
    • Teale, F.W.J.1
  • 32
    • 0019763671 scopus 로고
    • Preparation and properties of apohemoglobin and reconstituted hemoglobins
    • Ascoli, F., Fanelli, M. R., and Antonini, E. (1981) Preparation and properties of apohemoglobin and reconstituted hemoglobins Methods Enzymol. 76, 72-87
    • (1981) Methods Enzymol. , vol.76 , pp. 72-87
    • Ascoli, F.1    Fanelli, M.R.2    Antonini, E.3
  • 33
    • 0032513024 scopus 로고    scopus 로고
    • Immobilized apo-myoglobin, a new stable reagent for measuring rates of heme dissociation from hemoglobin
    • Gattoni, M., Boffi, A., and Chiancone, E. (1998) Immobilized apo-myoglobin, a new stable reagent for measuring rates of heme dissociation from hemoglobin FEBS Lett. 424, 275-278
    • (1998) FEBS Lett. , vol.424 , pp. 275-278
    • Gattoni, M.1    Boffi, A.2    Chiancone, E.3
  • 34
    • 0000980399 scopus 로고    scopus 로고
    • An Introduction to Research in Protein Folding for Undergraduates
    • Jones, C. M. (1997) An Introduction to Research in Protein Folding for Undergraduates J. Chem. Educ. 74, 1306
    • (1997) J. Chem. Educ. , vol.74 , pp. 1306
    • Jones, C.M.1
  • 35
    • 0011984231 scopus 로고    scopus 로고
    • Determination of Myoglobin Stability by Visible Spectroscopy
    • Sykes, P. A., Shiue, H.-C., Walker, J. R., and Bateman, R. C. (1999) Determination of Myoglobin Stability by Visible Spectroscopy J. Chem. Educ. 76, 1283
    • (1999) J. Chem. Educ. , vol.76 , pp. 1283
    • Sykes, P.A.1    Shiue, H.-C.2    Walker, J.R.3    Bateman, R.C.4
  • 36
    • 33947485233 scopus 로고
    • Nonpolar Group Participation in the Denaturation of Proteins by Urea and Guanidinium Salts. Model Compound Studies
    • Watlaufer, D. B., Malik, S. K., Stoller, L., and Coffin, R. L. (1964) Nonpolar Group Participation in the Denaturation of Proteins by Urea and Guanidinium Salts. Model Compound Studies J. Am. Chem. Soc. 86, 508-514
    • (1964) J. Am. Chem. Soc. , vol.86 , pp. 508-514
    • Watlaufer, D.B.1    Malik, S.K.2    Stoller, L.3    Coffin, R.L.4
  • 37
    • 68849132104 scopus 로고    scopus 로고
    • Molecular mechanism for the denaturation of proteins by urea
    • Almarza, J., Rincon, L., Bahsas, A., and Brito, F. (2009) Molecular mechanism for the denaturation of proteins by urea Biochemistry 48, 7608-7613
    • (2009) Biochemistry , vol.48 , pp. 7608-7613
    • Almarza, J.1    Rincon, L.2    Bahsas, A.3    Brito, F.4
  • 38
    • 0038370011 scopus 로고    scopus 로고
    • The molecular basis for the chemical denaturation of proteins by urea
    • Bennion, B. J. and Daggett, V. (2003) The molecular basis for the chemical denaturation of proteins by urea Proc. Natl. Acad. Sci. U.S.A. 100, 5142-5147
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 5142-5147
    • Bennion, B.J.1    Daggett, V.2
  • 39
    • 84875796365 scopus 로고    scopus 로고
    • Role of Polarity of the Distal Pocket in the Control of Inhibitor Binding in Dehaloperoxidase-Hemoglobin
    • Plummer, A., Thompson, M. K., and Franzen, S. (2013) Role of Polarity of the Distal Pocket in the Control of Inhibitor Binding in Dehaloperoxidase-Hemoglobin Biochemistry 52, 2218-2227
    • (2013) Biochemistry , vol.52 , pp. 2218-2227
    • Plummer, A.1    Thompson, M.K.2    Franzen, S.3
  • 40
    • 0017377521 scopus 로고
    • Disagreement between calorimetric and van't Hoff enthalpies of assembly of protein supramolecular structures
    • Sutherland, J. W. (1977) Disagreement between calorimetric and van't Hoff enthalpies of assembly of protein supramolecular structures Proc. Natl. Acad. Sci. U.S.A. 74, 2002-2006
    • (1977) Proc. Natl. Acad. Sci. U.S.A. , vol.74 , pp. 2002-2006
    • Sutherland, J.W.1
  • 41
    • 0024278461 scopus 로고
    • Calorimetric studies of the thermal denaturation of cytochrome c peroxidase
    • Kresheck, G. C. and Erman, J. E. (1988) Calorimetric studies of the thermal denaturation of cytochrome c peroxidase Biochemistry 27, 2490-2496
    • (1988) Biochemistry , vol.27 , pp. 2490-2496
    • Kresheck, G.C.1    Erman, J.E.2
  • 43
    • 0017253795 scopus 로고
    • Preparation of apohemoglobin trout IV and reconstitution with different hemes
    • Fioretti, E., Ascoli, F., and Brunori, M. (1976) Preparation of apohemoglobin trout IV and reconstitution with different hemes Biochem. Biophys. Res. Commun. 68, 1169-1173
    • (1976) Biochem. Biophys. Res. Commun. , vol.68 , pp. 1169-1173
    • Fioretti, E.1    Ascoli, F.2    Brunori, M.3
  • 46
    • 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., and Ghiladi, R. A. (2009) Characterization of Dehaloperoxidase Compound ES and Its Reactivity with Trihalophenols Biochemistry 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
  • 47
    • 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., and Franzen, S. (2007) 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. D63, 1094-1101
    • (2007) Acta Crystallogr. , vol.63 , pp. 1094-1101
    • De Serrano, V.1    Chen, Z.X.2    Davis, M.F.3    Franzen, S.4
  • 48
    • 84880547280 scopus 로고    scopus 로고
    • Kinetic Study of the Inhibition Mechanism of Dehaloperoxidase-Hemoglobin A by 4-Bromophenol
    • Zhao, J. and Franzen, S. (2013) Kinetic Study of the Inhibition Mechanism of Dehaloperoxidase-Hemoglobin A by 4-Bromophenol J. Phys. Chem. B 117, 8301-8309
    • (2013) J. Phys. Chem. B , vol.117 , pp. 8301-8309
    • Zhao, J.1    Franzen, S.2
  • 49
    • 37049135898 scopus 로고
    • Effect of 4-substitution on the thermodynamics of hydration of phenol and the phenoxide anion
    • Parsons, G. H., Rochester, C. H., and Wood, C. E. C. (1971) Effect of 4-substitution on the thermodynamics of hydration of phenol and the phenoxide anion J. Chem. Soc. B 533-536
    • (1971) J. Chem. Soc. B , pp. 533-536
    • Parsons, G.H.1    Rochester, C.H.2    Wood, C.E.C.3
  • 50
    • 0016505899 scopus 로고
    • The stability of globular proteins
    • Pace, C. N. (1975) The stability of globular proteins CRC Crit. Rev. Biochem. 3, 1-43
    • (1975) CRC Crit. Rev. Biochem. , vol.3 , pp. 1-43
    • Pace, C.N.1
  • 51
    • 0038644453 scopus 로고    scopus 로고
    • Equilibrium unfolding of RNase Rs from Rhizopus stolonifer: PH dependence of chemical and thermal denaturation
    • Deshpande, R. A., Khan, M. I., and Shankar, V. (2003) Equilibrium unfolding of RNase Rs from Rhizopus stolonifer: pH dependence of chemical and thermal denaturation Biochim. Biophys. Acta 1648, 184-194
    • (2003) Biochim. Biophys. Acta , vol.1648 , pp. 184-194
    • Deshpande, R.A.1    Khan, M.I.2    Shankar, V.3
  • 52
    • 0344739851 scopus 로고    scopus 로고
    • Kinetic inactivation study of mushroom tyrosinase: Intermediate detection by denaturants
    • Park, Y. D., Jung, J. Y., Kim, D. W., Kim, W. S., Hahn, M. J., and Yang, J. M. (2003) Kinetic inactivation study of mushroom tyrosinase: Intermediate detection by denaturants J. Protein Chem. 22, 463-471
    • (2003) J. Protein Chem. , vol.22 , pp. 463-471
    • Park, Y.D.1    Jung, J.Y.2    Kim, D.W.3    Kim, W.S.4    Hahn, M.J.5    Yang, J.M.6
  • 53
    • 0033819120 scopus 로고    scopus 로고
    • States of tryptophyl residues and stability of recombinant human matrix metalloproteinase 7 (matrilysin) as examined by fluorescence
    • Inouye, K., Tanaka, H., and Oneda, H. (2000) States of tryptophyl residues and stability of recombinant human matrix metalloproteinase 7 (matrilysin) as examined by fluorescence J. Biochem. 128, 363-369
    • (2000) J. Biochem. , vol.128 , pp. 363-369
    • Inouye, K.1    Tanaka, H.2    Oneda, H.3
  • 54
    • 0028960492 scopus 로고
    • How valid are denaturant-induced unfolding free energy measurements? Level of conformance to common assumptions over an extended range of ribonuclease A stability
    • Yao, M. and Bolen, D. W. (1995) How valid are denaturant-induced unfolding free energy measurements? Level of conformance to common assumptions over an extended range of ribonuclease A stability Biochemistry 34, 3771-3781
    • (1995) Biochemistry , vol.34 , pp. 3771-3781
    • Yao, M.1    Bolen, D.W.2
  • 55
    • 0032952722 scopus 로고    scopus 로고
    • Apohorseradish peroxidase unfolding and refolding: Intrinsic tryptophan fluorescence studies
    • Lasagna, M., Gratton, E., Jameson, D. M., and Brunet, J. E. (1999) Apohorseradish peroxidase unfolding and refolding: Intrinsic tryptophan fluorescence studies Biophys. J. 76, 443-450
    • (1999) Biophys. J. , vol.76 , pp. 443-450
    • Lasagna, M.1    Gratton, E.2    Jameson, D.M.3    Brunet, J.E.4
  • 56
    • 0034624966 scopus 로고    scopus 로고
    • Conversion of a c type cytochrome to a b type that spontaneously forms in vitro from apo protein and heme: Implications for c type cytochrome biogenesis and folding
    • Tomlinson, E. J. and Ferguson, S. J. (2000) Conversion of a c type cytochrome to a b type that spontaneously forms in vitro from apo protein and heme: Implications for c type cytochrome biogenesis and folding Proc. Natl. Acad. Sci. U.S.A. 97, 5156-5160
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 5156-5160
    • Tomlinson, E.J.1    Ferguson, S.J.2
  • 57
    • 0035843166 scopus 로고    scopus 로고
    • Improving enzymes by using them in organic solvents
    • Klibanov, A. M. (2001) Improving enzymes by using them in organic solvents Nature 409, 241-246
    • (2001) Nature , vol.409 , pp. 241-246
    • Klibanov, A.M.1
  • 58
  • 59
    • 34247576294 scopus 로고    scopus 로고
    • Globin gene family evolution and functional diversification in annelids
    • Bailly, X., Chabasse, C., Hourdez, S., Dewilde, S., Martial, S., Moens, L., and Zal, F. (2007) Globin gene family evolution and functional diversification in annelids FEBS J. 274, 2641-2652
    • (2007) FEBS J. , vol.274 , pp. 2641-2652
    • Bailly, X.1    Chabasse, C.2    Hourdez, S.3    Dewilde, S.4    Martial, S.5    Moens, L.6    Zal, F.7
  • 60
    • 0032052216 scopus 로고    scopus 로고
    • Hemoglobins from bacteria to man: Evolution of different patterns of gene expression
    • Hardison, R. (1998) Hemoglobins from bacteria to man: Evolution of different patterns of gene expression J. Exp. Biol. 201, 1099-1117
    • (1998) J. Exp. Biol. , vol.201 , pp. 1099-1117
    • Hardison, R.1
  • 62
    • 0030485204 scopus 로고    scopus 로고
    • Crystallization and initial spectroscopic characterization of the heme-containing dehaloperoxidase from the marine polychaete Amphitrite ornata
    • Zhang, E., Chen, Y. P., Roach, M. P., Lincoln, D. E., Lovell, C. R., Woodin, S. A., Dawson, J. H., and Lebioda, L. (1996) Crystallization and initial spectroscopic characterization of the heme-containing dehaloperoxidase from the marine polychaete Amphitrite ornata Acta Crystallogr. D52, 1191-1193
    • (1996) Acta Crystallogr. , vol.52 , pp. 1191-1193
    • Zhang, E.1    Chen, Y.P.2    Roach, M.P.3    Lincoln, D.E.4    Lovell, C.R.5    Woodin, S.A.6    Dawson, J.H.7    Lebioda, L.8
  • 64
    • 56449128760 scopus 로고    scopus 로고
    • Structural Reorganization and Preorganization in Enzyme Active Sites: Comparisons of Experimental and Theoretically Ideal Active Site Geometries in the Multistep Serine Esterase Reaction Cycle
    • Smith, A. J. T., Muller, R., Toscano, M. D., Kast, P., Hellinga, H. W., Hilvert, D., and Houk, K. N. (2008) Structural Reorganization and Preorganization in Enzyme Active Sites: Comparisons of Experimental and Theoretically Ideal Active Site Geometries in the Multistep Serine Esterase Reaction Cycle J. Am. Chem. Soc. 130, 15361-15373
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 15361-15373
    • Smith, A.J.T.1    Muller, R.2    Toscano, M.D.3    Kast, P.4    Hellinga, H.W.5    Hilvert, D.6    Houk, K.N.7
  • 65
    • 79959431109 scopus 로고    scopus 로고
    • Benchmark Reaction Rates, the Stability of Biological Molecules in Water, and the Evolution of Catalytic Power in Enzymes
    • In (Kornberg, R. D. Raetz, C. R. H. Rothman, J. E. and Thorner, J. W. Eds.) pp, Annual Reviews, Palo Alto, CA.
    • Wolfenden, R. (2011) Benchmark Reaction Rates, the Stability of Biological Molecules in Water, and the Evolution of Catalytic Power in Enzymes. In Annual Reviews of Biochemistry (Kornberg, R. D., Raetz, C. R. H., Rothman, J. E., and Thorner, J. W., Eds.) pp 645-667, Annual Reviews, Palo Alto, CA.
    • (2011) Annual Reviews of Biochemistry , pp. 645-667
    • Wolfenden, R.1
  • 66
    • 84891453216 scopus 로고    scopus 로고
    • Protein Conformational Disorder and Enzyme Catalysis
    • In (Klinman, J. and Hammes-Schiffer, S. Eds.) pp, Springer, Berlin.
    • Schulenburg, C. and Hilvert, D. (2013) Protein Conformational Disorder and Enzyme Catalysis. In Dynamics in Enzyme Catalysis (Klinman, J. and Hammes-Schiffer, S., Eds.) pp 41-67, Springer, Berlin.
    • (2013) Dynamics in Enzyme Catalysis , pp. 41-67
    • Schulenburg, C.1    Hilvert, D.2
  • 67
    • 84891356252 scopus 로고    scopus 로고
    • The regulatory implications of hydroquinone for the multifunctional enzyme dehaloperoxidase-hemoglobin from Amphitrite ornata
    • Zhao, J., Zhao, J., and Franzen, S. (2013) The regulatory implications of hydroquinone for the multifunctional enzyme dehaloperoxidase-hemoglobin from Amphitrite ornata J. Phys. Chem. B 117, 14615-14624
    • (2013) J. Phys. Chem. B , vol.117 , pp. 14615-14624
    • Zhao, J.1    Zhao, J.2    Franzen, S.3
  • 68
    • 0001202803 scopus 로고
    • The reaction of metmyoglobin with hydrogen peroxide
    • George, P. and Irvine, D. H. (1952) The reaction of metmyoglobin with hydrogen peroxide Biochem. J. 52, 511-517
    • (1952) Biochem. J. , vol.52 , pp. 511-517
    • George, P.1    Irvine, D.H.2
  • 69
    • 27744484001 scopus 로고
    • The Higher Oxidation State of Metmyoglobin
    • George, P. and Irvine, D. H. (1953) The Higher Oxidation State of Metmyoglobin Biochem. J. 53, R25
    • (1953) Biochem. J. , vol.53 , pp. 25
    • George, P.1    Irvine, D.H.2
  • 70
    • 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 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
  • 71
    • 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., and Lommel, S. A. (2006) Proximal cavity, distal histidine, and substrate hydrogen-bonding mutations modulate the activity of Amphitrite ornata dehaloperoxidase Biochemistry 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
  • 72
    • 80053039198 scopus 로고    scopus 로고
    • Amphitrite ornata Dehaloperoxidase (DHP): Investigations of Structural Factors That Influence the Mechanism of Halophenol Dehalogenation Using "peroxidase-like" Myoglobin Mutants and "myoglobin-like" DHP Mutants
    • Du, J., Huang, X., Sun, S. F., Wang, C. X., Lebioda, L., and Dawson, J. H. (2011) Amphitrite ornata Dehaloperoxidase (DHP): Investigations of Structural Factors That Influence the Mechanism of Halophenol Dehalogenation Using "Peroxidase-like" Myoglobin Mutants and "Myoglobin-like" DHP Mutants Biochemistry 50, 8172-8180
    • (2011) Biochemistry , vol.50 , pp. 8172-8180
    • Du, J.1    Huang, X.2    Sun, S.F.3    Wang, C.X.4    Lebioda, L.5    Dawson, J.H.6
  • 73
    • 84884497354 scopus 로고    scopus 로고
    • The role of T56 in controlling the flexibility of the distal histidine in dehaloperoxidase-hemoglobin from Amphitrite ornata
    • Jiang, S., Wright, I., Swartz, P., and Franzen, S. (2013) The role of T56 in controlling the flexibility of the distal histidine in dehaloperoxidase-hemoglobin from Amphitrite ornata Biochim. Biophys. Acta 1834, 2020-2029
    • (2013) Biochim. Biophys. Acta , vol.1834 , pp. 2020-2029
    • Jiang, S.1    Wright, I.2    Swartz, P.3    Franzen, S.4
  • 74
    • 84899437266 scopus 로고    scopus 로고
    • A Model for the Flexibility of the Distal Histidine in Dehaloperoxidase-Hemoglobin A Based on X-ray Crystal Structures of the Carbon Monoxide Adduct
    • Zhao, J., de Serrano, V., and Franzen, S. (2014) A Model for the Flexibility of the Distal Histidine in Dehaloperoxidase-Hemoglobin A Based on X-ray Crystal Structures of the Carbon Monoxide Adduct Biochemistry 53, 2474-2479
    • (2014) Biochemistry , vol.53 , pp. 2474-2479
    • Zhao, J.1    De Serrano, V.2    Franzen, S.3
  • 75
    • 58549116124 scopus 로고    scopus 로고
    • Distal histidine conformational flexibility in dehaloperoxidase from Amphitrite ornata
    • Chen, Z., De Serrano, V., Betts, L., and Franzen, S. (2009) Distal histidine conformational flexibility in dehaloperoxidase from Amphitrite ornata Acta Crystallogr. D65, 34-40
    • (2009) Acta Crystallogr. , vol.65 , pp. 34-40
    • Chen, Z.1    De Serrano, V.2    Betts, L.3    Franzen, S.4
  • 76
    • 84856420536 scopus 로고    scopus 로고
    • Thin-layer spectroelectrochemistry of the Fe(III)/Fe(II) redox reaction of dehaloperoxidase-hemoglobin
    • D'Antonio, E. L., Bowden, E. F., and Franzen, S. (2012) Thin-layer spectroelectrochemistry of the Fe(III)/Fe(II) redox reaction of dehaloperoxidase-hemoglobin J. Electroanal. Chem. 668, 37-43
    • (2012) J. Electroanal. Chem. , vol.668 , pp. 37-43
    • D'Antonio, E.L.1    Bowden, E.F.2    Franzen, S.3
  • 78
    • 84887599535 scopus 로고    scopus 로고
    • Functional consequences of the open distal pocket of dehaloperoxidase-hemoglobin observed by time-resolved X-ray crystallography
    • Zhao, J., Srajer, V., and Franzen, S. (2013) Functional consequences of the open distal pocket of dehaloperoxidase-hemoglobin observed by time-resolved X-ray crystallography Biochemistry 52, 7943-7950
    • (2013) Biochemistry , vol.52 , pp. 7943-7950
    • Zhao, J.1    Srajer, V.2    Franzen, S.3
  • 79
    • 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., and Hoffman, B. M. (2010) 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. 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
  • 81
    • 77954454306 scopus 로고    scopus 로고
    • X-ray structure of the metcyano form of dehaloperoxidase from Amphitrite ornata: Evidence for photoreductive dissociation of the iron-cyanide bond
    • de Serrano, V. S., Davis, M. F., Gaff, J. F., Zhang, Q., Chen, Z., D'Antonio, E. L., Bowden, E. F., Rose, R., and Franzen, S. (2010) X-ray structure of the metcyano form of dehaloperoxidase from Amphitrite ornata: Evidence for photoreductive dissociation of the iron-cyanide bond Acta Crystallogr. D66, 770-782
    • (2010) Acta Crystallogr. , vol.66 , pp. 770-782
    • De Serrano, V.S.1    Davis, M.F.2    Gaff, J.F.3    Zhang, Q.4    Chen, Z.5    D'Antonio, E.L.6    Bowden, E.F.7    Rose, R.8    Franzen, S.9
  • 82
    • 42949164473 scopus 로고    scopus 로고
    • EPR and ENDOR studies of cryoreduced compounds II of peroxidases and myoglobin. Proton-coupled electron transfer and protonation status of ferryl hemes
    • Davydov, R., Osborne, R. L., Kim, S. H., Dawson, J. H., and Hoffman, B. M. (2008) EPR and ENDOR studies of cryoreduced compounds II of peroxidases and myoglobin. Proton-coupled electron transfer and protonation status of ferryl hemes Biochemistry 47, 5147-5155
    • (2008) Biochemistry , vol.47 , pp. 5147-5155
    • Davydov, R.1    Osborne, R.L.2    Kim, S.H.3    Dawson, J.H.4    Hoffman, B.M.5


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