Biology 3602A/B Lecture Notes - Lecture 39: Glutathione Reductase, Unpaired Electron, Glutathione
5 Aug 2016
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Document Summary
Superoxide has the unpaired electron that makes it very reactive. Peroxide: add another electron to make it very reactive. Ros typically have an unpaired e- in outer orbital which makes them unstable. To stabilize outer orbital, they"ll steal e- from other molecs, and when it does that it"ll damage those molecs. Specifically, you can damage macromolecs like lipids, nucleic acids and proteins you can peroxidize them. Sod dismutes superoxides, and turns it from superoxide to h2o2 which is less reactive but still not great. So can further degrade h2o2 using cat that converts it into h2o and o2. Also take that h2o2 and use gpx which, using glutathione as a cofactor, produces water. Glutathione peroxidase reqs reduced glutathione, so glutathione reductase takes oxidized glutathione and reducing equivs like nadph to regenerate glutathione. We can also deal with them nonenzymatic nonenzymatic antioxidants aka free radical scavengers. These are compounds like vitamins e, and c, etc.
