000000599 001__ 599
000000599 005__ 20260112155011.0
000000599 0247_ $$2DOI$$a10.6083/M4G44N8H
000000599 037__ $$aETD
000000599 245__ $$aMechanistic studies of NO reduction in dinuclear metalloproteins
000000599 260__ $$bOregon Health and Science University
000000599 269__ $$a2011
000000599 336__ $$aDissertation
000000599 502__ $$bPh.D.
000000599 520__ $$aThis study investigates mechanisms by which metalloproteins reduce nitric oxide (NO) to nitrous oxide (N₂O), a key step in bacterial denitrification and nitrosative stress resistance. Using spectroscopic techniques, we show that NO binds first to heme iron(II) in terminal oxidases and engineered NOR models, while distal metals stabilize a heme-hyponitrite intermediate rather than directly binding NO. Flavodiiron proteins (FDPs) were also examined; deflavo-FDP retained single-turnover NO reduction, indicating the diiron center catalyzes NO reduction while FMN regenerates the oxidized site. These findings reveal distinct catalytic routes and roles of metal centers in NO reductase activity.
000000599 540__ $$fCC BY
000000599 542__ $$fIn copyright - single owner
000000599 650__ $$aSpectrum Analysis$$026223
000000599 650__ $$aDenitrification$$039179
000000599 650__ $$aOxidoreductases$$023422
000000599 650__ $$aIron Compounds$$039084
000000599 650__ $$aNitric Oxide$$022931
000000599 650__ $$aNitric Oxide Synthase$$031271
000000599 650__ $$aFourier Analysis$$019245
000000599 650__ $$aSpectrum Analysis, Raman$$026225
000000599 6531_ $$araman spectroscopy
000000599 6531_ $$adiiron
000000599 691__ $$aSchool of Medicine$$041369
000000599 692__ $$aDepartment of Environmental and Biomolecular Systems$$041414
000000599 7001_ $$aHayashi, Takahiro$$uOregon Health and Science University$$041354
000000599 7201_ $$aMoënne-Loccoz, Pierre$$uOregon Health and Science University$$041354$$7Personal$$eAdvisor
000000599 8564_ $$9fe0a33a3-32da-4d9b-94b3-861b5f2358a7$$s2883382$$uhttps://digitalcollections.ohsu.edu/record/599/files/600_etd.pdf$$ePublic$$2d7154731a414570bebe42d480f5948d0$$31
000000599 905__ $$a/rest/prod/q8/11/kj/61/q811kj61g
000000599 909CO $$ooai:digitalcollections.ohsu.edu:599$$pstudent-work
000000599 980__ $$aTheses and Dissertations