Work

Plasma membrane NADH‐coenzyme Q0 reductase generates semiquinone radicals and recycles vitamin E homologue in a superoxide‐dependent reaction

Year: 1998

Type: article

Abstract: We investigated the ability of plasma membrane CoQ reductase (PMQR) purified from pig liver to reduce phenoxyl radicals of a vitamin E homologue, Trolox. We report that NADH-driven one-electron reduction of CoQ0 catalyzed by PMQR produced CoQ0 semiquinone radical and CoQoH2. These in turn, recycle vitamin E homologue, Trolox, via reducing its phenoxyl radical. A significant part of NADH/PMQR-catalyzed reduction of CoQ0 (and Trolox recycling) was superoxide-dependent. Overall, our results demonstrate that PMQR in the model system used can act as an antioxidant enzyme that recycles water-soluble homologues of coenzyme Q and vitamin E.

Source: FEBS Letters

DOI: 10.1016/s0014-5793(98)00482-7

Authors: Valerian E Kagan, Antonio Arroyo, Vladimir A Tyurin, Yulia Y Tyurina, Jose M Villalba, Placido Navas

Institutions: University of Pittsburgh, University of Córdoba

Language: English

Topic: Coenzyme Q10 studies and effects

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funders: National Institutes of Health, National Institute of Neurological Disorders and Stroke

Awards: G706653329, OXIDATIVE STRESS--CELL OVEREXPRESSING AMYLOID PRECURSOR