Flavonoid-induced conversion of catalase to its inactive form-Compound II

• Published in: Free radical research Vol. 48; no. 11; pp. 1334 - 1341
• Main Authors: Krych, J., Gebicki, J. L., Gebicka, L.
• Format: Journal Article
• Language: English
• Published: England Informa Healthcare 01.11.2014; Taylor & Francis
• Subjects: Animals; catalase; Catalase - chemistry; Catalase - drug effects; Catalase - metabolism; Catalysis; Cattle; flavonoids; Flavonoids - pharmacology; Heme - chemistry; Heme - metabolism; heme proteins; Humans; Hydrogen Peroxide - metabolism; inhibitors; Models, Molecular; NADP - metabolism; Oxidants - metabolism; Oxidation-Reduction; oxidative stress; inhibitors; flavonoids; heme proteins; catalase; oxidative stress
• ISSN: 1071-5762; 1029-2470
• DOI: 10.3109/10715762.2014.953139

Abstract Flavonoids (FlaOHs), plant polyphenols, are ubiquitous components of human diet and are known as antioxidants. However, their prooxidant activity has also been reported. We have recently found that FlaOHs inhibit catalase, the heme enzyme which catalyzes the decomposition of hydrogen peroxide (H2O2) into water and molecular oxygen. The catalytic cycle proceeds with the formation of the intermediate, Compound I (Cpd I), an oxoferryl porphyrin π-cation radical, the two-electron oxidation product of a heme group. Under conditions of low H2O2 fluxes and in the presence of an appropriate substrate, Cpd I can undergo one-electron reduction to inactive Compound II (Cpd II), oxoferryl derivative without radical site. Here we show that in vitro, under low fluxes of H2O2, FlaOHs reduce Cpd I to inactive Cpd II. Measurable amounts of Cpd II can be formed even in the presence of reduced nicotinamide adenine dinucleotide phosphate (NADPH) at concentration comparable with the investigated FlaOHs. Possible mechanisms of electron transfer from FlaOH molecule to the heme are discussed.