View source for PMID:12682041

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!align=left  |Citation
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'''Lillig, CH, Potamitou, A, Schwenn, JD, Vlamis-Gardikas, A and Holmgren, A'''  (2003) Redox regulation of 3'-phosphoadenylylsulfate reductase from Escherichia coli by glutathione and glutaredoxins. ''J. Biol. Chem.'' '''278''':22325-30
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!align=left  |Abstract
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Inorganic sulfate (SO42-, S+VI) is reduced in vivo to sulfite (SO32-, S+IV) via phosphoadenylylsulfate (PAPS) reductase. Escherichia coli lacking glutathione reductase and glutaredoxins (gor-grxA-grxB-grxC-) barely grows on sulfate. We found that incubation of PAPS reductase with oxidized glutathione leads to enzyme inactivation with simultaneous formation of a mixed disulfide between glutathione and the active site Cys-239. A newly developed method based on thiol-specific fluorescent alkylation and gel electrophoresis showed that glutathionylated PAPS reductase is reduced by glutaredoxins via a monothiol mechanism. This glutathionylated species was also observed in poorly growing gor-grxA-grxB-grxC- cells expressing inactive glutaredoxin 2 (Grx2) C9S/C12S. However, it was absent in better growing cells expressing monothiol Grx2 C12S or wild type Grx2. Reversible glutathionylation may thus regulate the activity of PAPS reductase in vivo.
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!align=left  |Links
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=12682041 PubMed]
Online version:[http://dx.doi.org/10.1074/jbc.M302304200 10.1074/jbc.M302304200]
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!align=left  |Keywords
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Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/growth & development; Gene Deletion; Glutaredoxins; Glutathione/pharmacology; Glutathione Disulfide/pharmacology; Kinetics; Oxidoreductases/antagonists & inhibitors; Oxidoreductases/chemistry; Oxidoreductases/metabolism; Peptide Fragments/chemistry; Proteins/genetics; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Trypsin

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