We have determined for the first time, the thermodynamics of Fe3+ reduction for horseradish peroxidase (HRP-C), an enzyme containing a five-coordinate high-spin heme which catalyzes the oxidation of a wide variety of substrates by H2O2 or other organic peroxides and is the best known example of secretory plant heme-peroxidases. We have also measured the reduction enthalpy and entropy for the six-coordinate low-spin cyanide adduct. The E°¢ values of thesespecies at various temperatures have been obtained with a UVvis spectroelectrochemical approach.
Redox thermodynamics of the Fe3+/Fe2+ couple in horseradish peroxidase and its cyanide complex / Battistuzzi, Gianantonio; Borsari, Marco; Ranieri, Antonio; Sola, Marco. - In: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY. - ISSN 0002-7863. - STAMPA. - 124:1(2002), pp. 26-27. [10.1021/ja017188m]
Redox thermodynamics of the Fe3+/Fe2+ couple in horseradish peroxidase and its cyanide complex
BATTISTUZZI, Gianantonio;BORSARI, Marco;RANIERI, Antonio;SOLA, Marco
2002
Abstract
We have determined for the first time, the thermodynamics of Fe3+ reduction for horseradish peroxidase (HRP-C), an enzyme containing a five-coordinate high-spin heme which catalyzes the oxidation of a wide variety of substrates by H2O2 or other organic peroxides and is the best known example of secretory plant heme-peroxidases. We have also measured the reduction enthalpy and entropy for the six-coordinate low-spin cyanide adduct. The E°¢ values of thesespecies at various temperatures have been obtained with a UVvis spectroelectrochemical approach.
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