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 inhibition of soluble F1-ATPase indicates a direct interaction of the polyborate anion with the catalytic part of the enzyme molecule.
Drahota
Z
Z
Institute of Physiology, Academy of Sciences, Prague, Czech Republic.
Mares
V
V
Rauchová
H
H
Saf
P
P
Kalous
M
M
D000818:Animals; D001896:Boron Compounds / Q000737:chemistry / Q000494:pharmacology*; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000494:pharmacology*; D007700:Kinetics; D008930:Mitochondria, Liver / Q000201:enzymology*; D008958:Models, Molecular; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors*; D051381:Rats; D013329:Structure-Activity Relationship
D001896:Boron Compounds; D004791:Enzyme Inhibitors; D006180:Proton-Translocating ATPases