Inhibition of mitochondrial ATPase by dicarbopolyborate, a new enzyme inhibitor.

Authors

Drahota, Z; Mares, V; Rauchov?, H; Saf, P; Kalous, M

Publication Year 1994
Journal Journal of Bioenergetics and Biomembranes
Chapter
Pages 583-586
Volume 26
Issue 5
Issn
Isbn
PMID 7896773.0
PMCID
DOI 10.1007/BF00762743
URL http://dx.doi.org/10.1007/BF00762743

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.