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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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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
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Language:English
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description 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.
doi_str_mv 10.1007/BF00762743
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subjects Animals
Boron Compounds - chemistry
Boron Compounds - pharmacology
Enzyme Inhibitors - chemistry
Enzyme Inhibitors - pharmacology
Kinetics
Mitochondria, Liver - enzymology
Models, Molecular
Proton-Translocating ATPases - antagonists & inhibitors
Rats
Structure-Activity Relationship
title Inhibition of mitochondrial ATPase by dicarbopolyborate, a new enzyme inhibitor
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