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

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Author(s)
Yang, Chee; Greene, Alexander J.; Rauschnot, James C.
Advisor(s)
Hati, Sanchita; Bhattacharyay, Sudeep
Date
Apr 2009
Subject(s)
Oxidoreductases; Quinone reductases; Flavins; Posters
Series
USGZE AS589
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.
Description
Color poster with text, charts, and diagrams.
Sponsor(s)
University of Wisconsin--Eau Claire Office of Research and Sponsored Programs.
Permanent link
http://digital.library.wisc.edu/1793/36941 
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  • Student Research Day
    Posters of collaborative student/faculty research presented at Student Research Day

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