The mitochondrial inner-membrane anion channel possesses two mercurial-reactive regulatory sites.

European Journal of Biochemistry
Andrew D Beavis

Abstract

The mitochondrial inner membrane anion channel catalyzes the electrophoretic transport of a wide variety of anions and is inhibited by matrix divalent cations and protons. In this paper, evidence is provided that mersalyl and p-chloromercuribenzene-sulfonate each interact with this uniporter at two distinct sites. Binding to site 1 causes a shift in the pH dependence of transport, characterized by a decrease in the pIC50 for protons from about 7.8 to about 7.3, and leads to substantial stimulation of transport in the physiological pH range. This effect is not reversed by addition of thiols such as thioglycolate. Binding of mersalyl and p-chloromercuribenzenesulfonate to site 2 inhibits the transport of most anions including Pi, citrate, malonate, sulfate and ferrocyanide. The transport of Cl- is inhibited about 60% by mersalyl, but is not inhibited by p-chloromercuribenzenesulfonate. These data suggest that inhibition is a steric effect dependent on the size of the anion and the size of the R group of the mercurial. This inhibition is reversed by thioglycolate. Dose/response curves indicate that mersalyl binds to site 1 as the dose increased from 7 to 13 nmol/mg, whereas it binds to site 2 as the dose is increased from 10 to 18...Continue Reading

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Citations

Feb 1, 1992·Journal of Bioenergetics and Biomembranes·A D Beavis
Jun 1, 1996·The International Journal of Biochemistry & Cell Biology·P Jezek, J Borecký
May 31, 2008·Plant & Cell Physiology·Maura Nicoletta LausDonato Pastore
Nov 5, 2013·Antioxidants & Redox Signaling·Jin O-UchiShey-Shing Sheu
Apr 3, 2014·Physiological Reviews·Ildiko Szabo, Mario Zoratti
Jul 4, 1997·Biochimica Et Biophysica Acta·D W JungG P Brierley

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