User:Reuben Chacko
From Proteopedia
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One of the CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground. | One of the CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground. | ||
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| - | ""Glutathione"" | ||
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'''Glutathione reductase''' | '''Glutathione reductase''' | ||
| - | + | Glutathione reductase maintains a reducing environment inside cells by reducing glutathione disulfide to glutathione. Glutathione reductase or GSR catalyzes this reaction by attacking glutahione disulfide nucleophilically using its Cys63 residue. The Cys63 nucleophile itself is generated by the nucleophilic attack of FADH anion on the Cys58 - Cys63 disulfide bond. FADH anion in turn is generated by the reduction of FAD to FADH by NADPH. | |
| - | + | <applet load='1GRE' size='[450,438]' frame='true' align='center' caption='Glutathione reductase showing glutathione disulfide (molecule with two yellow spheres) and FAD with its flat flavin moiety sitting up-close ready to carry out the nucleophilic attack.'> | |
| - | <applet load='1GRE' size='[450,438]' frame='true' align='center' | + | |
| - | caption='Glutathione reductase showing glutathione disulfide (molecule with two yellow spheres) and FAD with its flat flavin moiety sitting up-close ready to carry out the nucleophilic attack.' | + | |
Revision as of 01:52, 1 May 2010
One of the CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground.
Glutathione reductase
Glutathione reductase maintains a reducing environment inside cells by reducing glutathione disulfide to glutathione. Glutathione reductase or GSR catalyzes this reaction by attacking glutahione disulfide nucleophilically using its Cys63 residue. The Cys63 nucleophile itself is generated by the nucleophilic attack of FADH anion on the Cys58 - Cys63 disulfide bond. FADH anion in turn is generated by the reduction of FAD to FADH by NADPH.
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