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Inhibition of mitochondrial ATPase by dicarbopolyborate, a new enzyme inhibitor

Polyborate anions were found to inhibit mitochondrial ATPase. Mercapto and chloro derivatives of dicarbononaborates showed full inhibition of the enzyme activity at 0.5-0.8 mM. The inhibitory effect of dodecaborates was lower. The inhibition was of competitive type with respect to ATP. The inhibitio...

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Bibliographic Details
Published in:Journal of bioenergetics and biomembranes 1994-10, Vol.26 (5), p.583-586
Main Authors: Drahota, Z, Mares, V, Rauchová, H, Saf, P, Kalous, M
Format: Article
Language:English
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Summary:Polyborate anions were found to inhibit mitochondrial ATPase. Mercapto and chloro derivatives of dicarbononaborates showed full inhibition of the enzyme activity at 0.5-0.8 mM. The inhibitory effect of dodecaborates was lower. The inhibition was of competitive type with respect to ATP. The inhibition of soluble F1-ATPase indicates a direct interaction of the polyborate anion with the catalytic part of the enzyme molecule.
ISSN:0145-479X
1573-6881
DOI:10.1007/BF00762743