Exploring Electron Transfer-Induced Conformational Changes in NRH:quinone Oxidoreductase.
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- Author(s)
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Yang, Chee; Greene, Alexander Jerome; Rauschnot, James C.
- Advisor(s)
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Hati, Sanchita; Bhattacharyay, Sudeep
- Date
- Apr 2009
- Subject(s)
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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
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