| Molecular mechanism of the reduction of cysteine sulfinic acid of peroxiredoxin to cysteine by mammalian sulfiredoxin. | |
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MedLine Citation:
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PMID: 16565085 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Among many proteins with cysteine sulfinic acid (Cys-SO2H) residues, the sulfinic forms of certain peroxiredoxins (Prxs) are selectively reduced by sulfiredoxin (Srx) in the presence of ATP. All Srx enzymes contain a conserved cysteine residue. To elucidate the mechanism of the Srx-catalyzed reaction, we generated various mutants of Srx and examined their interaction with PrxI, their ATPase activity, and their ability to reduce sulfinic PrxI. Our results suggest that three surface-exposed amino acid residues, corresponding to Arg50, Asp57, and Asp79 of rat Srx, are critical for substrate recognition. The presence of the sulfinic form (but not the reduced form) of PrxI induces the conserved cysteine of Srx to take the gamma-phosphate of ATP and then immediately transfers the phosphate to the sulfinic moiety of PrxI to generate a sulfinic acid phosphoryl ester (Prx-Cys-S(=O)OPO3(2-)). This ester is reductively cleaved by a thiol molecule (RSH) such as GSH, thioredoxin, and dithiothreitol to produce a disulfide-S-monoxide (Prx-Cys-S(=O)-S-R). The disulfide-S-monoxide is further reduced through the oxidation of three thiol equivalents to complete the catalytic cycle and regenerate Prx-Cys-SH. |
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Authors:
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Woojin Jeong; Sung Jun Park; Tong-Shin Chang; Duck-Yeon Lee; Sue Goo Rhee |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2006-03-24 |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 281 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 2006 May |
Date Detail:
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Created Date: 2006-05-15 Completed Date: 2006-07-21 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
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Languages: eng Pagination: 14400-7 Citation Subset: IM |
Affiliation:
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Laboratory of Cell Signaling, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Adenosine Diphosphate
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chemistry Adenosine Triphosphate / chemistry Animals Catalysis Cysteine / analogs & derivatives*, chemistry* Disulfides / chemistry Dithiothreitol / chemistry Humans Hydrolysis Models, Chemical Models, Molecular Mutation Oxidoreductases / chemistry* Oxidoreductases Acting on Sulfur Group Donors Peroxidases / chemistry* Peroxiredoxins Phosphates / chemistry Phosphorylation Rats |
| Chemical | |
Reg. No./Substance:
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0/Disulfides; 0/Phosphates; 2381-08-0/cysteine sulfinic acid; 3483-12-3/Dithiothreitol; 52-90-4/Cysteine; 56-65-5/Adenosine Triphosphate; 58-64-0/Adenosine Diphosphate; EC 1.-/Oxidoreductases; EC 1.11.1.-/Peroxidases; EC 1.11.1.15/Peroxiredoxins; EC 1.8.-/Oxidoreductases Acting on Sulfur Group Donors; EC 1.8.98.2/SRXN1 protein, human |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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