Amiloride inhibition of the proton‐translocating NADH‐quinone oxidoreductase of mammals and bacteria

FEBS Letters

Nakamaru-Ogiso, Eiko¹  Yagi, Takao¹  Seo, Byoung Boo¹  Matsuno-Yagi, Akemi¹ 

[1] Division of Biochemistry, Department of Molecular and Experimental Medicine, MEM-256, The Scripps Research Institute, 10550 Torrey Pines Road, La Jolla, CA 92037, USA

关键词: NADH dehydrogenase;    Amiloride derivative;    Q1;    ubiquinone-1;    NDH-1;    bacterial proton-translocating NADH-quinone oxidoreductase;    NDH-2;    NADH-quinone oxidoreductase lacking energy coupling;    complex I;    mitochondrial proton-translocating NADH-quinone oxidoreductase;    SMP;    submitochondrial particles;    EIPA;    5-(N-ethyl-N-isopropyl) amiloride;    MIA;    5-(N-methyl-N-isobutyl)amiloride;    TDF;    (trifluoromethyl)phenyldiazirinyl fenpyroximate;    PCR;    polymerase chain reaction;   

DOI  :  10.1016/S0014-5793(03)00766-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The proton-translocating NADH-quinone oxidoreductase in mitochondria (complex I) and bacteria (NDH-1) was shown to be inhibited by amiloride derivatives that are known as specific inhibitors for Na⁺/H⁺ exchangers. In bovine submitochondrial particles, the effective concentrations were about the same as those for the Na⁺/H⁺ exchangers, whereas in bacterial membranes the inhibitory potencies were lower. These results together with our earlier observation that the amiloride analogues prevent labeling of the ND5 subunit of complex I with a fenpyroximate analogue suggest the involvement of ND5 in H⁺ (Na⁺) translocation and no direct involvement of electron carriers in H⁺ (Na⁺) translocation.

【 授权许可】

Unknown