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Amiloride inhibition of the proton‐translocating NADH‐quinone oxidoreductase of mammals and bacteria
Author(s) -
Nakamaru-Ogiso Eiko,
Seo Byoung Boo,
Yagi Takao,
Matsuno-Yagi Akemi
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00766-x
Subject(s) - submitochondrial particle , amiloride , oxidoreductase , chemistry , quinone , biochemistry , bacteria , protein subunit , mitochondrion , stereochemistry , enzyme , biophysics , biology , sodium , organic chemistry , gene , genetics
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.