The thermodynamics of the one-electron reduction of the ferricheme in wild-type and mutated heme Synechocystis catalaseperoxidase and human myeloperoxidase were determined through spectro-electrochemical experiments. The data are interpreted in terms of ligand binding features, electrostatic effects and solvation properties of the heme environment.
Redox thermodynamics of the Fe3+/Fe2+ couple in wild type and mutated heme peroxidases / Battistuzzi, Gianantonio; Bellei, Marzia; C., Jakopitsch; J., Vlasits; P. G., Furtmüller; Sola, Marco; C., Obinger. - In: JBIC. - ISSN 0949-8257. - STAMPA. - 12:SUPPL 1(2007), pp. S62-S62. (Intervento presentato al convegno 13th International Conference on Biological Inorganic Chemistry (ICBIC XIII) tenutosi a Vienna (Austria) nel July 15-20 2007).
Redox thermodynamics of the Fe3+/Fe2+ couple in wild type and mutated heme peroxidases
BATTISTUZZI, Gianantonio;BELLEI, Marzia;SOLA, Marco;
2007
Abstract
The thermodynamics of the one-electron reduction of the ferricheme in wild-type and mutated heme Synechocystis catalaseperoxidase and human myeloperoxidase were determined through spectro-electrochemical experiments. The data are interpreted in terms of ligand binding features, electrostatic effects and solvation properties of the heme environment.
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