Abstract
Peroxidases catalyze the oxidation of a wide variety of organic compounds using hydrogen peroxide or other peroxides [1]. Reactions of peroxidases with H2O2 yield compound I structures that are two oxidizing equivalents above the resting ferric state. CompoundIVI of horseradish peroxidase (HRP) has been identified as a ferryl (Fe = 0) porphyrin radical cation [2] and is reduced by two single-electron transfers, first to compound II by the reduction of the porphyrin and subsequently to the resting ferric state.
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References
Dunford, H.B., Stillman, J.S., 1976, On the function and mechanism of action of peroxidases, Coord. Chem. Rev. 19: 187–251.
Penner-Hahn, J.B., Eble, K.S., Mc Murry, T.J., Renner, M., Balch, A.L., Groves, J.T., Dawson, J.H., Hogson, K.O., 1986, Structural characterization of horseradish peroxidase using EXAFS spectroscopy. Evidence for Fe=0 ligation in compound I and II, J. Am. Chem. Soc. 108: 7819#-7825.
Hager, L.P., Morris, D.R., Brown, F.S., Eberwein, H., 1966, Chloroperoxidase II. Utilisation of halogen anions, J. Biol. Chem. 241: 1769–1777.
Thomas, J.A., Morris, D.R., Hager, L.P., 1970, Chloroperoxidase VIII. Formation of peroxide and halide complexes and their relation to the mechanism of the halogenation reaction, J. Biol. Chem. 245: 3129–3134.
Kobayashi, S., Nakano, M., Goto, T., Kimura, T., Schaap, A.P., 1986, An evidence of the peroxidase-dependent oxygen transfer from hydrogen peroxide to sulfides, Biochem. Biophys. Res. Comm. 135: 166–171.
Ortiz de Montellano, P.R., Choe, Y.S., De Pillis, G., Catalano, C.E., 1987, Structure-mechanism relationships in hemoproteins, J. Biol. Chem. 262: 11641–11646.
Kobayashi, S., Nakano, M. Kimura, T., Schaap, A.P., 1987, On the mechanism of the peroxidase-catalyzed oxygen transfer reaccion, Biochemistry 26: 5019–5022.
Colonna, S., Gaggero, N., Manfredi, A., Casella, L., Gullotti, M., Carrea, G., Pasta, P., 1990, Enantioselective oxidations of sulfides catalyzed by chloroperoxidase, Biochemistry 29: 10465–10468.
Casella, L., Gullotti, M., Ghezzi, R., Poli, S., Beringhelli, T., Colonna, S., Carrea, G., submitted for publication.
Colonna, S., Gaggero, N., Carrea, G., Pasta, P., The horseradish peroxidase catalyzed sulfoxidation is enantioselective, J.C.S. Chem. Commun., in press.
Colonna, S., Gaggero, N., Casella, L., Carrea, G., Pasta, P., 1992, Chloroperoxidase and hydrogen peroxide: an efficient system for enzymatic enantioselective sulfoxidations, Tetrahedron Asymm. 3: 95–106.
Doerge, D.R., 1986, Oxygenation of organosulfur compounds by peroxidases: evidence of an electron transfer mechanism from lactoperoxidase, Arch. Biochem. Biophys. 678–685.
McCarty, M.B., White, R.E., 1983, Functional differences between peroxidase compound I and the cytochrome P-450 reactive oxygen intermediates, J. Biol. Chem. 258: 9153–9158.
Libby, R.D., Thomas, J.A., Kaiser, L.W., Hager, L.P., 1982, Chloroperoxidase halogenation reactions, J. Biol. Chem. 257: 5030–5037.
Samokyszyn, V.M., Ortiz de Montellano, P.R., 1991, Topology of the chloroperoxidase active site: regiospecificity of heme modification by phenylhydrazine and sodium azide, J. Biol. Chem. 11646–11653.
Perez, U., Dunford, H.B., 1990, Transiert-state kinetics of the reactions of l-methoxy-4(methylthio)benzene with horseradish peroxidase compounds I and II, Biochemistry 29: 2757–2763.
Doerge, D.R., Corbett, M.D., 1991, Peroxygenation mechanism for chloroperoxidase-catalyzed N-oxidation of arylamines, Chem. Res. Toxicol 556–560.
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© 1992 Springer Science+Business Media Dordrecht
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Colonna, S., Gaggero, N., Pasta, P. (1992). Enantioselective Sulfoxidations Catalyzed by Chloroperoxidase and Horseradish Peroxidase. In: Servi, S. (eds) Microbial Reagents in Organic Synthesis. NATO ASI Series, vol 381. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-2444-7_26
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DOI: https://doi.org/10.1007/978-94-011-2444-7_26
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