title: Catalase is inhibited by flavonoids.
abstract: Catalases, heme enzymes, which catalyze decomposition of hydrogen peroxide to water and molecular oxygen, belong to the antioxidant defense system of the cell. In this work we have shown that catalase from bovine liver is inhibited by flavonoids. The inhibition is, at least partially, due to the formation of hydrogen bonds between catalase and flavonoids. In the presence of some flavonoids the formation of unreactive catalase compound II has been detected. The most potent catalase inhibitors among the tested flavonoids have appeared myricetin, epicatechin gallate and epigallocatechin gallate. The relationship between the degree of enzyme inhibition and molecular structure of flavonoids has been analyzed.
authors.affiliation: Institute of Applied Radiation Chemistry, Faculty of Chemistry, Lodz University of Technology (TUL), Lodz, Poland.
authors.forename: Justyna
authors.initials: J
authors.lastname: Krych
authors.forename: Lidia
authors.initials: L
authors.lastname: Gebicka
mesh_terms: D000818:Animals; D002374:Catalase / Q000037:antagonists & inhibitors* / Q000737:chemistry; D002392:Catechin / Q000031:analogs & derivatives* / Q000737:chemistry; D002417:Cattle; D004791:Enzyme Inhibitors / Q000737:chemistry; D005419:Flavonoids / Q000737:chemistry; D006860:Hydrogen Bonding; D006861:Hydrogen Peroxide / Q000737:chemistry; D057927:Hydrophobic and Hydrophilic Interactions; D008099:Liver / Q000201:enzymology*
chemical_list: D004791:Enzyme Inhibitors; D005419:Flavonoids; C040015:myricetin; D002392:Catechin; C062669:epicatechin gallate; D006861:Hydrogen Peroxide; C045651:epigallocatechin gallate; D002374:Catalase; C057580:gallocatechol