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The dithiol-reactive reagent phenylarsine oxide causes a pH-dependent stimulation of unidirectional K+ flux into respiring rat liver mitochondria. This stimulation is diminished by subsequent addition of either the dithiol 2,3-dimercaptopropanol or the monothiol 2-mercaptoethanol. In contrast, uncoupling by phenylarsine oxide is reversed by 2,3-dimercaptopropanol but not by 2-mercaptoethanol. The data suggest separate sites of interaction of phenylarsine oxide with mechanisms of K+ entry and ATP synthesis. Stimulatory effects of mersalyl and phenylarsine oxide on K+ influx are not additive. Thus PheASO and mersalyl may affect K+ influx at a common site. Pretreatment of the mitochondria with DCCD, which inhibits K+ influx, fails to alter sensitivity to PheAsO or mersalyl. Thus the DCCD binding site associated with the K+ influx mechanism appears to be separate from and independent of the sulfhydryl group(s) which mediate stimulation of K+ influx by PheAsO and mersalyl. PheAsO, like mersalyl, also increases the rate of unidirectional K+ efflux from respiring mitochondria. The combined presence of PheAsO plus mersalyl causes a greater stimulation of K+ efflux than is observed with either reagent alone.

Effects on Mg++ transport in rat liver mitochondria of three reagents earlier shown to affect mitochondrial K+ transport have been examined. The sulfhydryl reactive reagent phenylarsine oxide, which activates K+ flux into respiring mitochondria, also stimulates Mg++ influx. The K+ analog Ba++, when taken up into the mitochondrial matrix, inhibits influx of both K+ and Mg++. The effect on Mg++ influx is seen only if Mg++, which blocks Ba++ accumulation, is added after a preincubation with Ba++. Thus the inhibition of Mg++ influx appears to require interaction of Ba++ at the matrix side of the inner mitochondrial membrane. Added Ba++ also diminishes observed rates of Mg++ efflux but not K+ efflux. This difference may relate to a higher concentration of Ba++ remaining in the medium in the presence of Mg++ under the conditions of our experiments. Pretreatment of mitochondria with dicyclohexyl-carbodiimide (DCCD), under conditions which result in an increase in the apparent Km for K+ of the K+ influx mechanism, results in inhibition of Mg++ influx from media containing approximately 0.2 mM Mg++. The inhibitory effect of DCCD on Mg++ influx is not seen at higher external Mg++ (0.8 mM). This dependence on cation concentration is similar to the dependence on K+ concentration of the inhibitory effect of DCCD on K+ influx. Although mitochondrial Mg++ and K+ transport mechanisms exhibit similar reagent sensitivities, whether Mg++ and K+ share common transport catalysis remains to be established.

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