The site of production of superoxide radical in mitochondrial Complex I is not a bound ubisemiquinone but presumably iron–sulfur cluster N2

FEBS Letters

Lenaz, Giorgio¹  Formiggini, Gabriella¹  Genova, Maria Luisa¹  Parenti Castelli, Giovanna¹  Giuliano, Giovanni¹  Ventura, Barbara¹  Bovina, Carla¹ 

[1] Dipartimento di Biochimica ‘G. Moruzzi’, Università di Bologna, Via Irnerio 48, 40126 Bologna, Italy

关键词: Coenzyme Q;    Complex I;    Iron–sulfur cluster;    Rotenone;    Submitochondrial particle;    Superoxide;    CoQ;    Coenzyme Q;    DB;    decyl-ubiquinone (2;    3-dimethoxy-5-methyl-6-decyl-1;    4-benzoquinone);    EDTA;    ethylenediaminetetraacetate;    HPLC;    high performance liquid chromatography;    ROS;    reactive oxygen species;    SMP;    submitochondrial particles;    SOD;    superoxide dismutase;   

DOI  :  10.1016/S0014-5793(01)02850-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The mitochondrial respiratory chain is a powerful source of reactive oxygen species, considered as the pathogenic agent of many diseases and of aging. We have investigated the role of Complex I in superoxide radical production in bovine heart submitochondrial particles and found, by combined use of specific inhibitors of Complex I and by Coenzyme Q (CoQ) extraction from the particles, that the one-electron donor in the Complex to oxygen is a redox center located prior to the binding sites of three different types of CoQ antagonists, to be identified with a Fe–S cluster, most probably N2 on the basis of several known properties of this cluster. Short chain CoQ analogs enhance superoxide formation, presumably by mediating electron transfer from N2 to oxygen. The clinically used CoQ analog, idebenone, is particularly effective in promoting superoxide formation.

【 授权许可】

Unknown