000002880 001__ 2880 000002880 005__ 20251104125012.0 000002880 0247_ $$2DOI$$a10.6083/M4XW4HJ2 000002880 037__ $$aETD 000002880 245__ $$aHistidine-methionine contributions to function in copper proteins 000002880 260__ $$bOregon Health and Science University 000002880 269__ $$a2015 000002880 336__ $$aDissertation 000002880 502__ $$bPh.D. 000002880 502__ $$gBiochemistry & Molecular Biology (sunsetting) 000002880 520__ $$aThe 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. 000002880 540__ $$fCC BY 000002880 542__ $$fIn copyright - single owner 000002880 650__ $$aCopper$$017086 000002880 650__ $$aBiological Transport$$015568 000002880 650__ $$aX-Ray Absorption Spectroscopy$$038773 000002880 650__ $$aBiochemistry$$015549 000002880 691__ $$aSchool of Medicine$$041369 000002880 692__ $$aInstitute of Environmental Health$$041473 000002880 7001_ $$aKline, Chelsey$$uOregon Health and Science University$$041354 000002880 7201_ $$aBlackburn, Ninian$$uOregon Health and Science University$$041354$$7Personal$$eAdvisor 000002880 7201_ $$aMayfield, Mary$$uOregon Health and Science University$$041354$$7Personal$$eMentor 000002880 8564_ $$942844da0-f6d7-45c4-bd74-792fa52f77b2$$s33967582$$uhttps://digitalcollections.ohsu.edu/record/2880/files/3649_etd.pdf$$ePublic$$29f1f7f11971045766566a705dd88b34d$$31 000002880 905__ $$a/rest/prod/8w/32/r5/85/8w32r585s 000002880 909CO $$ooai:digitalcollections.ohsu.edu:2880$$pstudent-work 000002880 980__ $$aTheses and Dissertations