FEBS Letters | |
Plasma membrane NADH‐coenzyme Q0 reductase generates semiquinone radicals and recycles vitamin E homologue in a superoxide‐dependent reaction | |
Navas, Placido2  Villalba, Jose M2  Arroyo, Antonio1  Tyurin, Vladimir A1  Tyurina, Yulia Y1  Kagan, Valerian E1  | |
[1] Department of Environmental and Occupational Health, University of Pittsburgh, 260 Kappa drive, Pittsburgh, PA 15238, USA;Departamento de Biologia Celular, Universidad de Cordoba, Cordoba, Spain | |
关键词: NADH-coenzyme Q0 reductase; Semiquinone radical; Vitamin E recycling; Superoxide; Coenzyme Q0; Trolox; PMQR; plasma membrane NADH-CoQ reductase; CoQ0; 2; 3-dimethoxy-5-methyl-1; 4 benzoquinone; ubiquinone Q0; CoQ0H2; ubiquinol Q0; DFO; deferoxamine mesylate; DOPC; l-alpha-phosphatidylcholine; dioleoyl (C18:1; [cis]-9) synthetic; SOD; superoxide dismutase; EPR; electron paramagnetic resonance; DMPO; 5; 5-dimethyl-1-pyrroline N-oxide; CHAPS; (3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate); | |
DOI : 10.1016/S0014-5793(98)00482-7 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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 CoQ0H2. 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.
【 授权许可】
Unknown
【 预 览 】
Files | Size | Format | View |
---|---|---|---|
RO201912020305963ZK.pdf | 163KB | download |