The pH-dependent anion-conducting channel of the mitochondrial inner membrane is potently inhibited by zinc ions.
Zinc is a potent reversible inhibitor of the pH-dependent anion-conducting channel in the mitochondrial inner membrane, 50% inhibition was produced by 1.5 microM added Zn2+ at which point free Zn2+ was < or = 10(-8) M. Inhibition by Zn2+ is rapid but can be prevented or rapidly reversed by excess EDTA. Concentrations of Zn2+ higher than 4 microM caused reversal of inhibition to a variable extent depending on the anion. Under these conditions Zn2+ did not inhibit ribose entry, the phosphate transporter, or the pH-insensitive component of the NO3- uniport.
Selwyn
M J
MJ
Department of Biochemistry, Faculty of Medicine, National University of Singapore.
Ng
L T
LT
Choo
H L
HL
D000818:Animals; D000838:Anions; D001692:Biological Transport; D002118:Calcium / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D007425:Intracellular Membranes / Q000187:drug effects* / Q000378:metabolism; D007473:Ion Channels / Q000187:drug effects*; D008274:Magnesium / Q000494:pharmacology; D008297:Male; D008930:Mitochondria, Liver / Q000187:drug effects* / Q000378:metabolism; D051381:Rats; D017208:Rats, Wistar; D012266:Ribose / Q000378:metabolism; D015032:Zinc / Q000494:pharmacology*
D000838:Anions; D007473:Ion Channels; D012266:Ribose; D008274:Magnesium; D015032:Zinc; D002118:Calcium