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Abstract
The goal of this research is to characterize the contribution of histidine and methionine to function in copper proteins. The emergence of His and Met residues in copper proteins is not new, but the flexible dynamic provided is novel and has been shown to alter function. We have characterized the pH-‐dependent coordination chemistry involving His-‐Met residues in cuproproteins peptidylglycine hydroxylating monooxygenase (PHM) and the HM Loop of ATP7A, which is involved in copper translocation.