Sandbox 181
From Proteopedia
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| - | Glutathione reductase, also known as GSH reductase, converts oxidized glutathione ( | + | Glutathione reductase, also known as GSH reductase, converts oxidized glutathione (GSSG) to two molecules of reduced [[gluthatione]] (GSH). |
== Structure == | == Structure == | ||
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== Reaction == | == Reaction == | ||
| - | The action of glutathione reductase proceeds through a cyclic series of structures in differing redox states (Figure 1). | + | The action of glutathione reductase proceeds through a cyclic series of structures in differing redox states (Figure 1). NADH binds causing a transient reduction of flavin and this reduced flavin consequently reduces Cys58-Cys63 disulfide bond, forming a short lived covalent intermediate with Cys63. Following this, a stable charge-transfer complex between flavin and the Cys63 thiolate. After this stable charge-transfer complex is formed the NADP+ dissociates and is replaced by another NADPH. This is the end of the reductive first half of the mechanism and the oxidative half is initiated upon the binding of GSSG. |
Revision as of 00:41, 19 March 2010
Glutathione reductase, also known as GSH reductase, converts oxidized glutathione (GSSG) to two molecules of reduced gluthatione (GSH).
Structure
Glutathione reductase belongs to the larger family of flavoezymes, which use a flavin adenine dinucleotide (FAD) or flavin mononucleotide (FMN) in catalysis. It is an oxiodrecutase homodimer of 52kD monomers of which, each has three domains: 1. NADPH-binding domain, 2. FAD-binding domain, 3. dimerization domain.
Reaction
The action of glutathione reductase proceeds through a cyclic series of structures in differing redox states (Figure 1). NADH binds causing a transient reduction of flavin and this reduced flavin consequently reduces Cys58-Cys63 disulfide bond, forming a short lived covalent intermediate with Cys63. Following this, a stable charge-transfer complex between flavin and the Cys63 thiolate. After this stable charge-transfer complex is formed the NADP+ dissociates and is replaced by another NADPH. This is the end of the reductive first half of the mechanism and the oxidative half is initiated upon the binding of GSSG.
Human Glutathione Reductase
| Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. Andrea Gorrell. |
