000008851 001__ 8851
000008851 005__ 20240124114311.0
000008851 0247_ $$2DOI$$a10.6083/fj2362777
000008851 037__ $$aETD
000008851 245__ $$aSpectroscopic and kinetic studies of histidine-methionine containing copper enzymes and proteins
000008851 260__ $$bOregon Health and Science University
000008851 269__ $$a2020
000008851 336__ $$aDissertation
000008851 502__ $$bPh.D.
000008851 520__ $$aThe Blackburn Lab studies biological copper chemistry using biochemical, biophysical, and advanced spectroscopic techniques. Our research aims are two-pronged, which is reflected in this dissertation. First, we aim to elucidate the mechanism of mononuclear copper monooxygenases, specifically peptidylglycine α-hydroxylating monooxygenase (PHM) and dopamine β-monooxygenase (DβM), both of which catalyze the hydroxylation of high energy C-H bonds utilizing a pair of chemically distinct copper sites (referred to as the M- and H- center) separated by 11 Å. The second research aim is to develop an understanding of the molecular basis of cuprous transport and export in the bacterial periplasmic efflux pump CusCBA and its metallochaperone CusF, which are vital to the detoxification of copper and silver ions in the periplasm of Escherichia coli.
000008851 542__ $$fIn copyright - single owner
000008851 650__ $$aCopper$$017086
000008851 650__ $$aSelenomethionine$$025837
000008851 650__ $$aX-Ray Absorption Spectroscopy$$038773
000008851 6531_ $$ametallochaperone
000008851 691__ $$aSchool of Medicine$$041369
000008851 7001_ $$aAlwan, Katherine B.
000008851 8564_ $$9296d5ae9-f2e1-40aa-ba19-ea25d467bed9$$s7093320$$uhttps://digitalcollections.ohsu.edu/record/8851/files/Alwan.Katherine.2020.pdf
000008851 905__ $$a/rest/prod/fj/23/62/77/fj2362777
000008851 909CO $$ooai:digitalcollections.ohsu.edu:8851$$pstudent-work
000008851 980__ $$aTheses and Dissertations