000002534 001__ 2534
000002534 005__ 20250501114040.0
000002534 0247_ $$2DOI$$a10.6083/M4QV3JTG
000002534 037__ $$aETD
000002534 245__ $$aSpectroscopic studies of peptidylglycine [alpha]-hydroxylating monooxygenase: toward a mechanism of superoxide channeling
000002534 260__ $$bOregon Health and Science University
000002534 269__ $$a2001-09-01
000002534 336__ $$aDissertation
000002534 502__ $$bPh.D.
000002534 520__ $$aThis dissertation describes the structural characterization of  peptidylglycine monooxygenase (PHM). PHM belongs to a unique class of  enzymes: the mononuclear dicopper monooxygenases. By  investigating the  structure and chemistry of  oxygen binding to the copper  sites in  PHM  and  its  active site mutants,  we  hope to gain an understanding of  the mechanism of  oxygen activation and electron transfer within this  enzyme class.
000002534 540__ $$fCC BY
000002534 542__ $$fIn copyright - single owner
000002534 650__ $$aReactive Oxygen Species$$029926
000002534 650__ $$aOxygen$$023434
000002534 650__ $$apeptidylglycine monooxygenase
000002534 691__ $$aOGI School of Science and Engineering$$041365
000002534 692__ $$aDepartment of Biochemistry and Molecular Biology$$041396
000002534 7001_ $$aShulamit, Jaron$$uOregon Health and Science University$$041354
000002534 7201_ $$aBlackburn, Ninian$$uOregon Health and Science University$$041354$$7Personal$$eAdvisor
000002534 8564_ $$9a48b3d8e-9209-42b4-87f0-3f229513b623$$s15797065$$uhttps://digitalcollections.ohsu.edu/record/2534/files/3277_etd.pdf$$ePublic$$2c0cc4337c743e259286ee83db62d6c94$$31
000002534 905__ $$a/rest/prod/3r/07/4v/14/3r074v14s
000002534 909CO $$ooai:digitalcollections.ohsu.edu:2534$$pstudent-work
000002534 980__ $$aTheses and Dissertations