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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. Amiloride inhibition of the proton-translocating NADH-quinone oxidoreductase of mammals and bacteria. Nakamaru-Ogiso, E., Seo, B.B., Yagi, T., Matsuno-Yagi, A. FEBS Lett. (2003) [Pubmed]
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