Spectroscopic evidence that salicylic acid converts a temporally inactivated form of horseradish peroxidase (compound III) to the irreversibly inactivated verdohemoprotein (P-670).
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.
Kawano
Tomonori
T
UMR INRA-UHP Interactions Arbre/Micro-Organismes, Centre Institut National de la Recherche Agronomique de Nancy, Champenoux, France. kawanotom@sci.hiroshima-u.ac.jp
Muto
Shoshi
S
Adachi
Masaru
M
Hosoya
Hiroshi
H
Lapeyrie
Frédéric
F
D004578:Electron Spin Resonance Spectroscopy; D005609:Free Radicals / Q000737:chemistry; D006420:Hemeproteins / Q000737:chemistry*; D006735:Horseradish Peroxidase / Q000737:chemistry*; D006861:Hydrogen Peroxide / Q000737:chemistry; D010940:Plant Proteins; D020156:Salicylic Acid / Q000737:chemistry*; D013055:Spectrophotometry, Infrared
D005609:Free Radicals; D006420:Hemeproteins; C023351:P-670 verdohemoprotein, plant; D010940:Plant Proteins; D006861:Hydrogen Peroxide; D006735:Horseradish Peroxidase; D020156:Salicylic Acid