Abstract
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. © 2002 by Japan Society for Bioscience, Biotechnology, and Agrochemistry.
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Kawano, T., Muto, S., Adachi, M., Hosoya, H., & Lapeyrie, F. (2002). Spectroscopic evidence that salicylic acid converts a temporally inactivated form of horseradish peroxidase (Compound III) to the irreversibly inactivated verdohemoprotein (P-670). Bioscience, Biotechnology and Biochemistry, 66(3), 646–650. https://doi.org/10.1271/bbb.66.646
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