ISSN:
1573-6881
Keywords:
H+-ATP synthase
;
mitochondrial F0-F1 complex
;
ATPase
;
H+-translocation
;
alkyl cations
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Physics
Notes:
Abstract The amphiphylic alkyl cation cetyltrimethylammonium inhibits the catalytic activity of soluble and membrane-bound F1 in a noncompetitive fashion. In sonic submitochondrial particles the Dixon plot showed a peculiar pattern with upward deviation at cetyltrimethylammonium concentration higher than 80µM. In membrane-bound F1 the inhibition by cetyltrimethylammonium was potentiated by the F0 inhibitor ologomycin. Cetyltrimethylammonium also inhibited the oligomycin-sensitive proton conductivity in F1-containing particles but was without any effect in F1-depleted particles. Also this inhibitory effect was potentiated by oligomycin. These results indicate functional cooperative interactions between F0 and F1.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00762730
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