The mammalian peroxidases participate in host defence against infection, hormone synthesis and pathogenesis. The most striking feature of these heme enzymes is the existence of two covalent ester bonds between the prosthetic group and the protein in the functional, mature proteins. Myeloperoxidase is unique in having an additional vinyl-sulfonium bond. The impact of heme distortion and asymmetry on the spectral and enzymatic properties is discussed as is the role of the MPO-typical electron withdrawing sulfonium ion linkage in raising the reduction potential of its redox intermediatesand maintaining a rigid solvent network at the distal heme cavity.
Impact of heme to protein linkages in peroxidases on redox chemistry and catalysis / C., Obinger; J., Vlasits; Bellei, Marzia; Battistuzzi, Gianantonio; P. G., Furtmüller. - In: JBIC. - ISSN 0949-8257. - STAMPA. - 12:SUPPL 1(2007), pp. S59-S59. (Intervento presentato al convegno 13th International Conference on Biological Inorganic Chemistry (ICBIC XIII) tenutosi a Vienna (Austria) nel July 15-20 2007).
Impact of heme to protein linkages in peroxidases on redox chemistry and catalysis
BELLEI, Marzia;BATTISTUZZI, Gianantonio;
2007
Abstract
The mammalian peroxidases participate in host defence against infection, hormone synthesis and pathogenesis. The most striking feature of these heme enzymes is the existence of two covalent ester bonds between the prosthetic group and the protein in the functional, mature proteins. Myeloperoxidase is unique in having an additional vinyl-sulfonium bond. The impact of heme distortion and asymmetry on the spectral and enzymatic properties is discussed as is the role of the MPO-typical electron withdrawing sulfonium ion linkage in raising the reduction potential of its redox intermediatesand maintaining a rigid solvent network at the distal heme cavity.
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