NADH and NADPH-Dependent Reduction of Coenzyme Q at the Plasma Membrane

被引：34

作者：

Arroyo, Antonio ^{[1
,2
,3
]}

Kagan, Valerian E. ^{[2
,3
]}

Tyurin, Vladimir A. ^{[2
,3
]}

Burgess, John R. ^{[4
]}

de Cabo, Rafael ^{[4
]}

Navas, Placido ^{[5
]}

Villalba, Jose M. ^{[1
]}

机构：

[1] Univ Cordoba, Fac Ciencias, Dept Biol Celular Fisiol & Immunol, E-14071 Cordoba, Spain

[2] Univ Pittsburgh, Dept Environm & Occupat Hlth, Pittsburgh, PA USA

[3] Univ Pittsburgh, Dept Pharmacol, Pittsburgh, PA 15261 USA

[4] Purdue Univ, Dept Foods & Nutr, W Lafayette, IN 47907 USA

[5] Univ Pablo de Olavide, Lab Andaluz Biol, Seville, Spain

来源：

ANTIOXIDANTS & REDOX SIGNALING | 2000年 / 2卷 / 02期

关键词：

D O I：

10.1089/ars.2000.2.2-251

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

High affinity for NADH, and low affinity for NADPH, for reduction of endogenous coenzyme Q(10) (CoQ(10)) by pig liver plasma membrane is reported in the present work. CoQ reduction in plasma membrane is carried out, in addition to other mechanisms, by plasma membrane coenzyme Q reductase (PMQR). W e show that PMQR-catalyzed reduction of CoQ(0) by both NADH and NADPH is accompanied by generation of CoQ(0) semiquinone radicals in a superoxide-dependent reaction. In the presence of a water-soluble vitamin E homologue, Trolox, this reduction leads to quenching of the Trolox phenoxyl radicals. The involvement of PMQR versus DT-diaphorase under the conditions of vitamin E and selenium sufficiency and deficiency was evaluated for CoQ reduction by plasma membranes. The data presented here suggest that both nucleotides (NADH and NADPH) can be accountable for CoQ reduction by PMQR on the basis of their physiological concentrations within the cell. The enzyme is primarily responsible for CoQ reduction in plasma membrane under normal (nonoxidative stress-associated) conditions. Antiox. Redox Signal. 2, 251-262.

引用

页码：251 / 262

页数：12

共 31 条

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