Energetics of Hydride Transfer Reactions in Quinone Reductase 2

dc.contributor.advisorHati, Sanchita
dc.contributor.advisorBhattacharyya, Sudeep
dc.contributor.authorYang, Yer
dc.contributor.authorBartholow, Thomas G.
dc.contributor.authorNorth, Michael A.
dc.date.accessioned2012-10-03T19:23:59Z
dc.date.available2012-10-03T19:23:59Z
dc.date.issued2012-04
dc.descriptionColor poster with text, images, diagrams, charts, graphs, and tables.en
dc.description.abstractQuinone Reductases belong to the class of flavin-dependent oxidoreductases. With its redox active cofactor flavin adenine dinucleotide (FAD), quinone reductases are known to utilize a ping pong kinetic mechanism during catalysis in which a hydride is swapped back and forth between flavin and its two substrates. The objectives of this study were: to explore the energetics of the ping pong kinetics in NQO2; to examine the conformational changes and free energy change due to substrate shuttling; and to determine the best functional to calculate the electron interaction.en
dc.description.sponsorshipUniversity of Wisconsin--Eau Claire Office of Research and Sponsored Programs.en
dc.identifier.urihttp://digital.library.wisc.edu/1793/63156
dc.language.isoen_USen
dc.relation.ispartofseriesUSGZE AS589en
dc.subjectChemical kineticsen
dc.subjectQuinoneen
dc.subjectFlavinsen
dc.subjectOxidoreductasesen
dc.subjectPostersen
dc.titleEnergetics of Hydride Transfer Reactions in Quinone Reductase 2en
dc.typePresentationen

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