Abstract
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.
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