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. 1988 Jul 15;253(2):371–376. doi: 10.1042/bj2530371

A novel aspect of the inhibition by arsenicals of binding-protein-dependent galactose transport in gram-negative bacteria.

G Richarme 1
PMCID: PMC1149308  PMID: 3052423

Abstract

The inhibitory effects of arsenate and arsenite on binding-protein-dependent transport systems are reconsidered. It is shown that arsenate inhibits binding-protein-dependent galactose transport in proteoliposomes energized either by dihydrolipoamide and NAD+ or by a membrane potential (under conditions where ATP metabolism is not implicated); this result is in contradiction with the current interpretation of arsenate inhibition of binding-protein-dependent transport systems (which is based on ATP depletion) and can be explained by reference to the recently discovered ATP inhibition of the binding-protein-dependent galactose transport. In whole cells, the greater inhibition by arsenate of lipoamide-dependent transport than of protonmotive-force-dependent transport may be explained by a modification by arsenate of the pools of several compounds metabolized by 2-oxo-acid dehydrogenases (which have been implicated in binding-protein-dependent transport). The inhibition of binding-protein-dependent galactose transport by arsenite is probably linked to the inhibition by arsenite of the galactose-stimulated lipoamide dehydrogenase activity implicated in this transport and is reminiscent of the known arsenite inhibition of lipoamide dehydrogenases.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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