Exploring Electron Transfer-Induced Conformational Changes in NRH:quinone Oxidoreductase.

dc.contributor.advisor	Hati, Sanchita
dc.contributor.advisor	Bhattacharyay, Sudeep
dc.contributor.author	Yang, Chee
dc.contributor.author	Greene, Alexander J.
dc.contributor.author	Rauschnot, James C.
dc.date.accessioned	2009-09-25T17:51:50Z
dc.date.available	2009-09-25T17:51:50Z
dc.date.issued	2009-04
dc.description	Color poster with text, charts, and diagrams.	en
dc.description.abstract	NRH:quinone oxidoreductase is a flavoenzyme that catalyzes the one-step reduction of quinones to hydroquinones using its cofactor, FAD. The enzyme kinetics goes through a "ping-pong" mechanism, in which changes in the flavin redox state control substrate binding and release. In this study, we are studying the slower dynamics of the subunit interface (surrounding the active site) using Normal Mode Analysis and exploring its relationship with the faster local motions.	en
dc.description.sponsorship	University of Wisconsin--Eau Claire Office of Research and Sponsored Programs.	en
dc.identifier.uri	http://digital.library.wisc.edu/1793/36941
dc.language.iso	en_US	en
dc.relation.ispartofseries	USGZE AS589	en
dc.subject	Oxidoreductases	en
dc.subject	Quinone reductases	en
dc.subject	Flavins	en
dc.subject	Posters	en
dc.title	Exploring Electron Transfer-Induced Conformational Changes in NRH:quinone Oxidoreductase.	en
dc.type	Presentation	en

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