Bacterial chromosomes have genes for transport of inorganic nutrient cations (such as NH
4+, K
+, Mg
2+, Co
2+, Fe
3+, Mn
2+, Zn
2+ and other trace cations) and oxyanions (such as PO
43- and SO
42- and less abundant oxyanions). Together these account for sometimes several hundred genes in many bacteria. Bacterial plasmids encode resistance systems for toxic metal and metalloid ions including Ag
+, AsO
2-, AsO
43-, Cd
2+, Co
2+, CrO
42-, Cu
2+, Hg
2+, Ni
2+, Pb
2+, Sb
3+, TeO
32-, Tl
+, and Zn
2+. Most resistance systems function by energy-dependent efflux of toxic ions. A few involve enzymatic (mostly redox) transformants. Some of the efflux resistance systems are ATPases and others are chemiosmotic ion/proton exchangers. Mercury resistance is due to enzymatic detoxification with organomercurial lyase (cutting the C-Hg bond of compounds such as methylmercury and phenylmercury) and mercuric reductase (Hg
2+→Hg
0). The Cd
2+-resistance cation P-type ATPases of Gram-positive bacteria drives Cd
2+ (and Zn
2+) efflux from resistant cells. The genes defective in the human hereditary diseases of copper metabolism, Menkes syndrome and Wilson's disease, encode Cu-specific P-type ATPases that are similar to bacterial Cd
2+ ATPases. The arsenic resistance system transports arsenite [As(III)], alternatively with the ArsB protein functioning as a chemiosmotic efflux transporter or with two proteins, ArsB and ArsA, functioning as an ATPase transporter. The third protein of the arsenic resistance system is an enzyme that reduces intracellular arsenate [As(V)] to arsenite [As(III)], the substrate of the efflux system. In Gram negative cells, a three polypeptide complex functions as a chemiosmotic cation/proton exchanger to efflux Cd
2+, Zn
2+, and Co
2+. This pump consists of an inner membrane (CzcA), an outer membrane (CzcC) and a membrane-spanning (CzcB) protein that function together.
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