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Mechanism Of Cu+-Transporting Atpases: Soluble Cu+ Chaperones Directly Transfer Cu+ To Transmembrane Transport Sites, José Argüello, Manuel Gonzalez-Guerrero

José M. Argüello

As in other P-type ATPases, metal binding to transmembrane metal-binding sites (TM-MBS) in Cu(+)-ATPases is required for enzyme phosphorylation and subsequent transport. However, Cu(+) does not access Cu(+)-ATPases in a free (hydrated) form but is bound to a chaperone protein. Cu(+) transfer from Cu(+) chaperones to regulatory cytoplasmic metal-binding domains (MBDs) present in these ATPases has been described, but there is no evidence of a proposed subsequent Cu(+) movement from the MBDs to the TM-MBS. Alternatively, we postulate the parsimonious Cu(+) transfer by the chaperone directly to TM-MBS. Testing both models, the delivery of Cu(+) by Archaeoglobus fulgidus Cu(+) chaperone …