Spectroscopic Evidence That Salicylic Acid Converts a Temporally Inactivated Form of Horseradish Peroxidase (Compound III) to the Irreversibly Inactivated Verdohemoprotein (P-670)
UMR INRA-UHP Interactions Arbre/Micro-Organismes, Centre Institut National de la Recherche Agronomique de NancyPresent address: Department of Biological Science, Graduate School of Science, Hiroshima University
Shoshi MUTO
Nagoya University Bioscience Center
Masaru ADACHI
Department of Biochemistry, Miyazaki Medical College
Hiroshi HOSOYA
Department of Biological Science, Graduate School of Science and PRESTO-JST, Hiroshima University
Frédéric LAPEYRIE
UMR INRA-UHP Interactions Arbre/Micro-Organismes, Centre Institut National de la Recherche Agronomique de Nancy
We obtained spectroscopic evidence in support of salicylate-dependent inactivation of horseradish peroxidase-C. Addition of salicylate to the enzyme arrested at a temporal inactive state (Compound III) in the presence of H2O2, resulted in rapid and irreversible inactivation of the enzyme yielding verdohemoproteins (P-670). Multiple roles for salicylate in peroxidase- catalyzed reactions are discussed.
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