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Volumn 50, Issue 41, 2011, Pages 8926-8936

A heme peroxidase with a functional role as an l -tyrosine hydroxylase in the biosynthesis of anthramycin

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC AMINO ACID; BIOSYNTHESIS GENE CLUSTER; CATALYTIC EFFICIENCIES; COFACTORS; DITYROSINE; HEME IRON; HEME PEROXIDASE; HORSE-RADISH PEROXIDASE; HYDROXYLASES; HYDROXYLATION OF PHENOL; L-DOPA PRODUCTIONS; L-TYROSINE; OXIDATION REACTIONS; PRE-INCUBATION; PUTATIVE FUNCTIONS; REACTION BEHAVIOR; SPECTROSCOPIC DATA; STEADY-STATE KINETICS; SUBSTRATE SPECIFICITY; TYROSINE HYDROXYLASE; UV-VIS SPECTRUM;

EID: 80054756991     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201148a     Document Type: Article
Times cited : (36)

References (58)
  • 1
    • 84857665235 scopus 로고    scopus 로고
    • Biosynthesis, synthesis, and biological activities of pyrrolobenzodiazepines
    • 10.1002/med.20212
    • Gerratana, B. (2011) Biosynthesis, synthesis, and biological activities of pyrrolobenzodiazepines Med. Res. Rev. 10.1002/med.20212
    • (2011) Med. Res. Rev.
    • Gerratana, B.1
  • 2
    • 2542430327 scopus 로고    scopus 로고
    • Lincomycin, clindamycin and their applications
    • DOI 10.1007/s00253-003-1545-7
    • Spízek, J. and Rezanka, T. (2004) Lincomycin, clindamycin and their applications Appl. Microbiol. Biotechnol. 64, 455-464 (Pubitemid 38686153)
    • (2004) Applied Microbiology and Biotechnology , vol.64 , Issue.4 , pp. 455-464
    • Spizek, J.1    Rezanka, T.2
  • 4
    • 0018634219 scopus 로고
    • Pyrrolo[1,4]benzodiazepine antibiotics. Biosynthetic conversion of tyrosine to the C2- and C3-proline moieties of anthramycin, tomaymycin, and sibiromycin
    • Hurley, L. H., Lasswell, W. L., Ostrander, J. M., and Parry, R. (1979) Pyrrolo[1,4]benzodiazepine antibiotics. Biosynthetic conversion of tyrosine to the C2- and C3-proline moieties of anthramycin, tomaymycin, and sibiromycin Biochemistry 18, 4230-4237
    • (1979) Biochemistry , vol.18 , pp. 4230-4237
    • Hurley, L.H.1    Lasswell, W.L.2    Ostrander, J.M.3    Parry, R.4
  • 5
    • 0021734217 scopus 로고
    • Biosynthesis of the lincomycins. 1. Studies using stable isotopes on the biosynthesis of the propyl- anbd ethyl-L-hygric acid moieties of lincomycins A and B
    • DOI 10.1021/ja00337a038
    • Brahme, N. M., Gonzalez, J. E., Rolls, J. P., Hessler, E. J., Mizsak, S., and Hurley, L. H. (1984) Biosynthesis of the lincomycins. 1. Studies using stable isotopes on the biosynthesis of the propyl- and ethyl-L-hygric acid moieties of lincomycins A and B J. Am. Chem. Soc. 106, 7873-7878 (Pubitemid 15193801)
    • (1984) Journal of the American Chemical Society , vol.106 , Issue.25 , pp. 7873-7878
    • Brahme, N.M.1    Gonzalez, J.E.2    Rolls, J.P.3
  • 6
    • 79953058897 scopus 로고    scopus 로고
    • Insights into the Biosynthesis of Hormaomycin, An Exceptionally Complex Bacterial Signaling Metabolite
    • Höfer, I., Crüsemann, M., Radzom, M., Geers, B., Flachshaar, D., Cai, X., Zeeck, A., and Piel, J. (2011) Insights into the Biosynthesis of Hormaomycin, An Exceptionally Complex Bacterial Signaling Metabolite Chem. Biol. 18, 381-391
    • (2011) Chem. Biol. , vol.18 , pp. 381-391
    • Höfer, I.1    Crüsemann, M.2    Radzom, M.3    Geers, B.4    Flachshaar, D.5    Cai, X.6    Zeeck, A.7    Piel, J.8
  • 7
    • 0029084746 scopus 로고
    • Molecular characterization of the lincomycin-production gene cluster of Streptomyces lincolnensis 78-11
    • Peschke, U., Schmidt, H., Zhang, H.-Z., and Piepersberg, W. (1995) Molecular characterization of the lincomycin-production gene cluster of Streptomyces lincolnensis 78-11 Mol. Microbiol. 16, 1137-1156
    • (1995) Mol. Microbiol. , vol.16 , pp. 1137-1156
    • Peschke, U.1    Schmidt, H.2    Zhang, H.-Z.3    Piepersberg, W.4
  • 8
    • 4544261979 scopus 로고    scopus 로고
    • L-3,4-dihydroxyphenyl alanine-extradiol cleavage is followed by intramolecular cyclization in lincomycin biosynthesis
    • DOI 10.1111/j.1432-1033.2004.04308.x
    • Novotna, J., Honzatko, A., Bednar, P., Kopecky, J., Janata, J., and Spizek, J. (2004) L-3,4-Dihydroxyphenyl alanine-extradiol cleavage is followed by intramolecular cyclization in lincomycin biosynthesis Eur. J. Biochem. 271, 3678-3683 (Pubitemid 39233610)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.18 , pp. 3678-3683
    • Novotna, J.1    Honzatko, A.2    Bednar, P.3    Kopecky, J.4    Janata, J.5    Spizek, J.6
  • 9
    • 0031594596 scopus 로고    scopus 로고
    • The genes ImbB1 and ImbB2 of Streptomyces lincolnensis encode enzymes involved in the conversion of L-tyrosine to propylproline during the biosynthesis of the antibiotic lincomycin A
    • DOI 10.1007/s002030050578
    • Neusser, D., Schmidt, H., Spizek, J., Novotna, J., U., P., Kaschabeck, S., Tichy, P., and Piepersberg, W. (1998) The genes lmbB1 and lmbB2 of Streptomyces lincolnensis encode enzymes involved in the conversion of L-tyrosine to propylproline during the biosynthesis of the antibiotic lincomycin A Arch. Microbiol. 169, 322-332 (Pubitemid 28189536)
    • (1998) Archives of Microbiology , vol.169 , Issue.4 , pp. 322-332
    • Neusser, D.1    Schmidt, H.2    Spizek, J.3    Novotna, J.4    Peschke, U.5    Kaschabeck, S.6    Tichy, P.7    Piepersberg, W.8
  • 10
    • 34250628482 scopus 로고    scopus 로고
    • Benzodiazepine Biosynthesis in Streptomyces refuineus
    • DOI 10.1016/j.chembiol.2007.05.009, PII S1074552107001780
    • Hu, Y., Phelan, V., Ntai, I., Farnet, C. M., Zazopoulos, E., and Bachmann, B. O. (2007) Benzodiazepine Biosynthesis in Streptomyces refuineus Chem. Biol. 14, 691-701 (Pubitemid 46929091)
    • (2007) Chemistry and Biology , vol.14 , Issue.6 , pp. 691-701
    • Hu, Y.1    Phelan, V.2    Ntai, I.3    Farnet, C.M.4    Zazopoulos, E.5    Bachmann, B.O.6
  • 11
    • 65549162526 scopus 로고    scopus 로고
    • Cloning and Characterization of the Biosynthetic Gene Cluster of Tomaymycin, an SJG-136 monomeric analog
    • Li, W., Chou, S., Khullar, A., and Gerratana, B. (2009) Cloning and Characterization of the Biosynthetic Gene Cluster of Tomaymycin, an SJG-136 monomeric analog Appl. Environ. Microbiol. 75, 2958-2963
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 2958-2963
    • Li, W.1    Chou, S.2    Khullar, A.3    Gerratana, B.4
  • 14
    • 0141448799 scopus 로고    scopus 로고
    • Evolution of the soluble diiron monooxygenases
    • DOI 10.1016/S0168-6445(03)00023-8
    • Leahy, J. G., Batchelor, P. J., and Morcomb, S. M. (2003) Evolution of the soluble diiron monooxygenases FEMS. Microbiol. Rev. 27, 449-479 (Pubitemid 37205164)
    • (2003) FEMS Microbiology Reviews , vol.27 , Issue.4 , pp. 449-479
    • Leahy, J.G.1    Batchelor, P.J.2    Morcomb, S.M.3
  • 15
    • 0345492036 scopus 로고    scopus 로고
    • Mechanism of Aromatic Amino Acid Hydroxylation
    • DOI 10.1021/bi035656u
    • Fitzpatrick, P. F. (2003) Mechanism of Aromatic Amino Acid Hydroxylation Biochemistry 42, 14083-14091 (Pubitemid 37499404)
    • (2003) Biochemistry , vol.42 , Issue.48 , pp. 14083-14091
    • Fitzpatrick, P.F.1
  • 16
    • 34547778115 scopus 로고    scopus 로고
    • Structural insights into dioxygen-activating copper enzymes
    • Rosenzweig, A. C. and Sazinsky, M. H. (2006) Structural insights into dioxygen-activating copper enzymes Curr. Opin. Struct. Biol. 16, 729
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 729
    • Rosenzweig, A.C.1    Sazinsky, M.H.2
  • 17
    • 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
    • (2007) Cell. Mol. Life. Sci. , vol.64 , pp. 271
    • Ullrich, R.1    Hofrichter, M.2
  • 18
    • 17644413773 scopus 로고    scopus 로고
    • The 2-His-1-carboxylate facial triad: A versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes
    • DOI 10.1007/s00775-005-0624-x
    • Koehntop, K. D., Emerson, J. P., and Que, L. (2005) The 2-His-1-carboxylate facial triad: a versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes J. Biol. Inorg. Chem. 10, 87-93 (Pubitemid 40569003)
    • (2005) Journal of Biological Inorganic Chemistry , vol.10 , Issue.2 , pp. 87-93
    • Koehntop, K.D.1    Emerson, J.P.2    Que Jr., L.3
  • 19
    • 33845959112 scopus 로고    scopus 로고
    • An Escherichia coli expression-based method for heme substitution
    • DOI 10.1038/nmeth984, PII NMETH984
    • Woodward, J. J., Martin, N. I., and Marletta, M. A. (2007) An Escherichia coli expression-based method for heme substitution Nature Methods 4, 43-45 (Pubitemid 46029474)
    • (2007) Nature Methods , vol.4 , Issue.1 , pp. 43-45
    • Woodward, J.J.1    Martin, N.I.2    Marletta, M.A.3
  • 20
    • 0023653927 scopus 로고
    • Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra
    • Berry, E. A. and Trumpower, B. L. (1987) Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra Anal. Biochem. 161, 1-15
    • (1987) Anal. Biochem. , vol.161 , pp. 1-15
    • Berry, E.A.1    Trumpower, B.L.2
  • 21
    • 38049026202 scopus 로고    scopus 로고
    • Assay of tyrosine hydroxylase based on high-performance liquid chromatography separation and quantification of L-dopa and L-tyrosine
    • Olsovská, J., Novotná, J., Flieger, M., and Spízek, J. (2007) Assay of tyrosine hydroxylase based on high-performance liquid chromatography separation and quantification of L-dopa and L-tyrosine Biomed. Chromatogr. 21, 1252-1258
    • (2007) Biomed. Chromatogr. , vol.21 , pp. 1252-1258
    • Olsovská, J.1    Novotná, J.2    Flieger, M.3    Spízek, J.4
  • 22
    • 0001544080 scopus 로고
    • The Properties of Thyroglobulin
    • Edelhoch, H. (1962) The Properties of Thyroglobulin J. Biol. Chem. 237, 2778-2787
    • (1962) J. Biol. Chem. , vol.237 , pp. 2778-2787
    • Edelhoch, H.1
  • 23
    • 80054763883 scopus 로고    scopus 로고
    • The Merck Index, 13 th ed. entry # 5485.
    • The Merck Index, 13 th ed., entry # 5485.
  • 25
    • 0000435509 scopus 로고
    • Colormetric Determination of the Components of 3,4- dihydroxyphenylalanine-tyrosine Mixtures
    • Arnow, L. E. (1937) Colormetric Determination of the Components of 3,4-dihydroxyphenylalanine-tyrosine Mixtures J. Biol. Chem. 118, 531-537
    • (1937) J. Biol. Chem. , vol.118 , pp. 531-537
    • Arnow, L.E.1
  • 26
    • 0025777217 scopus 로고
    • Steady-state kinetic mechanism of rat tyrosine hydroxylase
    • Fitzpatrick, P. F. (1991) Steady-state kinetic mechanism of rat tyrosine hydroxylase Biochemistry 30, 3658-3662
    • (1991) Biochemistry , vol.30 , pp. 3658-3662
    • Fitzpatrick, P.F.1
  • 27
    • 0029557684 scopus 로고
    • Kinetics of Oxidation of Tyrosine and Dityrosine by Myeloperoxidase Compounds i and II
    • Marquez, L. A. and Dunford, H. B. (1995) Kinetics of Oxidation of Tyrosine and Dityrosine by Myeloperoxidase Compounds I and II J. Biol. Chem. 270, 30434-30440
    • (1995) J. Biol. Chem. , vol.270 , pp. 30434-30440
    • Marquez, L.A.1    Dunford, H.B.2
  • 28
    • 38049022793 scopus 로고
    • Non-Enzymatic Oxidation of Tyrosine and Dopa
    • Morris, F. (1950) Non-Enzymatic Oxidation of Tyrosine and Dopa Proc. Natl. Acad. Sci. U. S. A. 36, 606-611
    • (1950) Proc. Natl. Acad. Sci. U. S. A. , vol.36 , pp. 606-611
    • Morris, F.1
  • 30
    • 0029737895 scopus 로고    scopus 로고
    • The association rate constant for heme binding to globin is independent of protein structure
    • DOI 10.1021/bi960371l
    • Hargrove, M. S., Barrick, D., and Olson, J. S. (1996) The Association Rate Constant for Heme Binding to Globin Is Independent of Protein Structure Biochemistry 35, 11293-11299 (Pubitemid 26299302)
    • (1996) Biochemistry , vol.35 , Issue.35 , pp. 11293-11299
    • Hargrove, M.S.1    Barrick, D.2    Olson, J.S.3
  • 31
    • 0029892404 scopus 로고    scopus 로고
    • Stability of the heme-globin linkage in ab dimers and isolated chains of human hemoglobin. A study of the heme transfer reaction from the immobilized proteins to albumin
    • Gattoni, M., Boffi, A., Sarti, P., and Chiancone, E. (1996) Stability of the heme-globin linkage in ab dimers and isolated chains of human hemoglobin. A study of the heme transfer reaction from the immobilized proteins to albumin J. Biol. Chem. 271, 10130-10136
    • (1996) J. Biol. Chem. , vol.271 , pp. 10130-10136
    • Gattoni, M.1    Boffi, A.2    Sarti, P.3    Chiancone, E.4
  • 32
    • 33749010088 scopus 로고    scopus 로고
    • The mechanism of heme transfer from the cytoplasmic heme binding protein PhuS to the δ-regioselective heme oxygenase of Pseudomonas aeruginosa
    • DOI 10.1021/bi060980l
    • Bhakta, M. N. and Wilks, A. (2006) The Mechanism of Heme Transfer from the Cytoplasmic Heme Binding Protein PhuS to the δ-Regioselective Heme Oxygenase of Pseudomonas aeruginosa Biochemistry 45, 11642-11649 (Pubitemid 44454011)
    • (2006) Biochemistry , vol.45 , Issue.38 , pp. 11642-11649
    • Bhakta, M.N.1    Wilks, A.2
  • 33
    • 0022423905 scopus 로고
    • Spectroscopic examination of the active site of bovine ferrochelatase
    • Dailey, H. A. (1985) Spectroscopic examination of the active site of bovine ferrochelatase Biochemistry. 24, 1287-1291
    • (1985) Biochemistry. , vol.24 , pp. 1287-1291
    • Dailey, H.A.1
  • 34
    • 0034043337 scopus 로고    scopus 로고
    • 5
    • DOI 10.1006/prep.2000.1228
    • Mulrooney, S. B. and Waskell, L. (2000) High-Level Expression in Escherichia coli and Purification of the Membrane-Bound Form of Cytochrome b5 Protein Expression Purif. 19, 173-178 (Pubitemid 30387908)
    • (2000) Protein Expression and Purification , vol.19 , Issue.1 , pp. 173-178
    • Mulrooney, S.B.1    Waskell, L.2
  • 35
    • 33845995083 scopus 로고    scopus 로고
    • Structure of the Escherichia coli O157:H7 heme oxygenase ChuS in complex with heme and enzymatic inactivation by mutation of the heme coordinating residue His-193
    • DOI 10.1074/jbc.M607684200
    • Suits, M. D. L., Jaffer, N., and Jia, Z. (2006) Structure of the Escherichia coli O157:H7 Heme Oxygenase ChuS in Complex with Heme and Enzymatic Inactivation by Mutation of the Heme Coordinating Residue His-193 J. Biol. Chem. 281, 36776-36782 (Pubitemid 46042145)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.48 , pp. 36776-36782
    • Suits, M.D.L.1    Jaffer, N.2    Jia, Z.3
  • 37
    • 42749090328 scopus 로고    scopus 로고
    • Heme content of recombinant catalase from Psychrobacter sp. T-3 altered by host Escherichia coli cell growth conditions
    • Kimoto, H., Matsuyama, H., Yumoto, I., and Yoshimune, K. (2008) Heme content of recombinant catalase from Psychrobacter sp. T-3 altered by host Escherichia coli cell growth conditions Protein Expression Purif. 59, 357-359
    • (2008) Protein Expression Purif. , vol.59 , pp. 357-359
    • Kimoto, H.1    Matsuyama, H.2    Yumoto, I.3    Yoshimune, K.4
  • 40
    • 84863872700 scopus 로고    scopus 로고
    • Catalytic Mechanisms of Heme Peroxidases
    • in (Torres, E. and Ayala, M. Eds.) Springer-Verlag, Berlin.
    • Ortiz de Montellano, P. R. (2010) Catalytic Mechanisms of Heme Peroxidases, in Biocatalysis Based on Heme Peroxidases (Torres, E. and Ayala, M., Eds.) Springer-Verlag, Berlin.
    • (2010) Biocatalysis Based on Heme Peroxidases
    • Ortiz De Montellano, P.R.1
  • 41
    • 80054762860 scopus 로고    scopus 로고
    • A Compendium of Bio-Physical-Chemical Properties of Peroxidases
    • in (Torres, E. and Ayala, M. Eds.) Springer-Verlag, Berlin.
    • Garcia-Arellano, H. (2010) A Compendium of Bio-Physical-Chemical Properties of Peroxidases, in Biocatalysis Based on Heme Peroxidases (Torres, E. and Ayala, M., Eds.) Springer-Verlag, Berlin.
    • (2010) Biocatalysis Based on Heme Peroxidases
    • Garcia-Arellano, H.1
  • 42
    • 0023053393 scopus 로고
    • Horseradish Peroxidase Catalyzed Hydroxylations: Mechanistic Studies
    • Dordick, J. S., Klibanov, A. M., and Marletta, M. A. (1986) Horseradish Peroxidase Catalyzed Hydroxylations: Mechanistic Studies Biochemistry 25, 2946-2951
    • (1986) Biochemistry , vol.25 , pp. 2946-2951
    • Dordick, J.S.1    Klibanov, A.M.2    Marletta, M.A.3
  • 43
    • 0017412726 scopus 로고
    • Generation of hydrogen peroxide, superoxide and hydroxyl radicals during the oxidation of dihydroxyfumaric acid by peroxidase
    • Halliwell, B. (1977) Generation of Hydogen Peroxide, Superoxide, and Hydroxyl Radicals during the Oxidation of Dihydroxyfumaric acid by Peroxidase Biochem. J. 163, 441-448 (Pubitemid 8125762)
    • (1977) Biochemical Journal , vol.163 , Issue.3 , pp. 441-448
    • Halliwell, B.1
  • 44
    • 0028361241 scopus 로고
    • The chloroperoxidase-catalyzed oxidation of phenols. Mechanism, selectivity, and characterization of enzyme-substrate complexes
    • DOI 10.1021/bi00187a001
    • Casella, L., Gullotti, M., Selvaggini, C., Poli, S., Beringhelli, T., and Marchesini, A. (1994) The Chloroperoxidase-Catalyzed Oxidation of Phenols. Mechanism, Selectivity, and Characterization of Enzyme-Substrate Complexes Biochemistry 33, 6377-6386 (Pubitemid 24189346)
    • (1994) Biochemistry , vol.33 , Issue.21 , pp. 6377-6386
    • Casella, L.1    Poli, S.2    Gullotti, M.3    Selvaggini, C.4    Beringhelli, T.5    Marchesini, A.6
  • 45
    • 0027417395 scopus 로고
    • Dityrosine, a specific marker of oxidation, is synthesized by the myeloperoxidase-hydrogen peroxide system of human neutrophils and macrophages
    • Heinecke, J. W., Li, W., Daehnke, H. L., and Goldstein, J. A. (1993) Dityrosine, a specific marker of oxidation, is synthesized by the myeloperoxidase-hydrogen peroxide system of human neutrophils and macrophages J. Biol. Chem. 268, 4069-4077 (Pubitemid 23072943)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.6 , pp. 4069-4077
    • Heinecke, J.W.1    Li, W.2    Daehnke III, H.L.3    Goldstein, J.A.4
  • 46
    • 78149373621 scopus 로고    scopus 로고
    • Cytochrome P450 Compound I: Capture, Characterization, and C-H Bond Activation Kinetics
    • Rittle, J. and Green, M. T. (2010) Cytochrome P450 Compound I: Capture, Characterization, and C-H Bond Activation Kinetics Science 330, 933-937
    • (2010) Science , vol.330 , pp. 933-937
    • Rittle, J.1    Green, M.T.2
  • 47
    • 0037174181 scopus 로고    scopus 로고
    • Functional modulation of a peroxygenase cytochrome P450: Novel insight into the mechanisms of peroxygenase and peroxidase enzymes
    • DOI 10.1016/S0014-5793(02)03261-1, PII S0014579302032611
    • Matsunaga, I., Sumimoto, T., Ayata, M., and Ogura, H. (2002) Functional modulation of a peroxygenase cytochrome P450: novel insight into the mechanisms of peroxygenase and peroxidase enzymes FEBS Lett. 528, 90-94 (Pubitemid 35258005)
    • (2002) FEBS Letters , vol.528 , Issue.1-3 , pp. 90-94
    • Matsunaga, I.1    Sumimoto, T.2    Ayata, M.3    Ogura, H.4
  • 49
    • 44949255484 scopus 로고    scopus 로고
    • Electron transfer activation of chromopyrrolic acid by cytochrome P450 en route to the formation of an antitumor indolocarbazole derivative: Theory supports experiment
    • DOI 10.1021/ja711426y
    • Wang, Y., Hirao, H., Chen, H., Onaka, H., Nagano, S., and Shaik, S. (2008) Electron Transfer Activation of Chromopyrrolic Acid by Cytochrome P450 En Route to the Formation of an Antitumor Indolocarbazole Derivative: Theory Supports Experiment J. Am. Chem. Soc. 130, 7170-7171 (Pubitemid 351813178)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.23 , pp. 7170-7171
    • Wang, Y.1    Hirao, H.2    Chen, H.3    Onaka, H.4    Nagano, S.5    Shaik, S.6
  • 50
    • 0038110968 scopus 로고    scopus 로고
    • A proton-shuttle mechanism mediated by the porphyrin in benzene hydroxylation by cytochrome P450 enzymes
    • DOI 10.1021/ja034142f
    • de Visser, S. P. and Shaik, S. (2003) A Proton-Shuttle Mechanism Mediated by the Porphyrin in Benzene Hydroxylation by Cytochrome P450 Enzymes J. Am. Chem. Soc. 125, 7413-7424 (Pubitemid 36798988)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.24 , pp. 7413-7424
    • De Visser, S.P.1    Shaik, S.2
  • 53
    • 0028901185 scopus 로고
    • Crystal structure of recombinant pea cytosolic ascorbate peroxidase
    • Patterson, W. R. and Poulos, T. L. (1995) Crystal structure of recombinant pea cytosolic ascorbate peroxidase Biochemistry 34, 4331-4341
    • (1995) Biochemistry , vol.34 , pp. 4331-4341
    • Patterson, W.R.1    Poulos, T.L.2
  • 56
    • 84895263475 scopus 로고    scopus 로고
    • Deactivation of Hemeperoxidases by Hydrogen Peroxide: Focus on Compound III
    • in (Torres, E. and Ayala, M. Eds.) Springer-Verlag, Berlin.
    • Valderrama, B. (2010) Deactivation of Hemeperoxidases by Hydrogen Peroxide: Focus on Compound III, in Biocatalysis Based on Heme Peroxidases (Torres, E. and Ayala, M., Eds.) Springer-Verlag, Berlin.
    • (2010) Biocatalysis Based on Heme Peroxidases
    • Valderrama, B.1
  • 57
    • 61449121236 scopus 로고    scopus 로고
    • Characterization of Dehaloperoxidase Compound ES and Its Reactivity with Trihalophenols
    • Feducia, J., Dumarieh, R., Gilvey, L. B., 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.3    Smirnova, T.4    Franzen, S.5    Ghiladi, R.A.6
  • 58
    • 77954310525 scopus 로고    scopus 로고
    • An analysis of substrate binding interactions in the heme peroxidase enzymes: A structural perspective
    • Gumiero, A., Murphy, E., Metcalfe, C. L., Moody, P., and Raven, E. L. (2010) An analysis of substrate binding interactions in the heme peroxidase enzymes: A structural perspective Arch. Biochem. Biophys. 500, 13-20
    • (2010) Arch. Biochem. Biophys. , vol.500 , pp. 13-20
    • Gumiero, A.1    Murphy, E.2    Metcalfe, C.L.3    Moody, P.4    Raven, E.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.