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Originally published In Press as doi:10.1074/jbc.M001507200 on March 27, 2000

J. Biol. Chem., Vol. 275, Issue 22, 16767-16773, June 2, 2000
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Cation Hexaammines Are Selective and Potent Inhibitors of the CorA Magnesium Transport System*

Lisa M. KucharskiDagger , Wil J. Lubbe, and Michael E. Maguire

From the Department of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106-4965

Cation hexaammines and related compounds are chemically stable analogs of the hydrated form of cations, particularly Mg2+. We tested the ability of several of these compounds to inhibit transport by the CorA or MgtB Mg2+ transport systems or the PhoQ receptor kinase for Mg2+ in Salmonella typhimurium. Cobalt(III)-, ruthenium(II)-, and ruthenium(III)-hexaammines were potent inhibitors of CorA-mediated influx. Cobalt(III)- and ruthenium(III)chloropentaammines were slightly less potent inhibitors of CorA. The compounds inhibited uptake by the bacterial S. typhimurium CorA and by the archaeal Methanococcus jannaschii CorA, which bear only 12% identity in the extracellular periplasmic domain. Cation hexaammines also inhibited growth of S. typhimurium strains dependent on CorA for Mg2+ uptake but not of isogenic strains carrying a second Mg2+ uptake system. In contrast, hexacyano-cobaltate(III) and ruthenate(II)- and nickel(II)hexaammine had little effect on uptake. The inhibition by the cation hexaammines was selective for CorA because none of the compounds had any effect on transport by the MgtB P-type ATPase Mg2+ transporter or the PhoQ Mg2+ receptor kinase. These results demonstrate that cation hexaammines are potent and highly selective inhibitors of the CorA Mg2+ transport system and further indicate that the initial interaction of the CorA transporter is with a fully hydrated Mg2+ cation.

* This work was supported by National Institutes of Health Grant GM39447 (to M.E.M.) and a summer undergraduate fellowship from the American Society of Pharmacology and Experimental Therapeutics (to W. J. L.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Dept. of Pharmacology, School of Medicine, Case Western Reserve University, 10900 Euclid Ave., Cleveland, OH 44106-4965. Tel.: 216-368-6187; Fax: 216-368-3395; E-mail: lmk10@po.cwru.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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