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