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Glutaredoxins catalyze the reduction of glutathione by dihydrolipoamide with high efficiency
- Source :
- Biochemical and Biophysical Research Communications. 295:1046-1051
- Publication Year :
- 2002
- Publisher :
- Elsevier BV, 2002.
-
Abstract
- Glutaredoxins (Grx) are small (approximately 12kDa) proteins which catalyze thiol disulfide oxidoreductions involving glutathione (GSH) and disulfides in proteins or small molecules. Here, we present data which demonstrate the ability of glutaredoxins to catalyze the reduction of oxidized glutathione (GSSG) by dihydrolipoamide (DHL), an important biological redox catalyst and synthetic antioxidant. We have designed a new assay method to quantify the rate of reduction of GSSG and other disulfides by reduced lipoamide and have tested a set of eight recombinant Grx from human, rat, yeast, and E. coli. Lipoamide dependent activity is highest with the large atypical E. coli Grx2 (k(cat)=3.235 min(-1)) and lowest for human mitochondrial Grx2a (k(cat)=96 min(-1)) covering a wider range than k(cat) for the standard reduction of hydroxyethyldisulfide (HED) by GSH (290-2.851 min(-1)). The lipoamide/HED activity ratio was highest for yeast Grx2 (1.25) and E. coli Grx2 and lowest for E. coli Grx1 (0.13). These results suggest a new role for Grxs as ancillary proteins that could shunt reducing equivalents from main catabolic pathways to recycling of GSSG via a lipoyl group, thus serving biochemical functions which involve GSH but without NAD(P)H consumption.
- Subjects :
- Antioxidant
Dihydrolipoamide
medicine.medical_treatment
Biophysics
medicine.disease_cause
Biochemistry
Catalysis
chemistry.chemical_compound
Glutaredoxin
Escherichia coli
medicine
Animals
Molecular Biology
Glutaredoxins
Thioctic Acid
Proteins
Cell Biology
Glutathione
Recombinant Proteins
Yeast
Rats
chemistry
Lipoamide
NAD+ kinase
Oxidoreductases
Oxidation-Reduction
medicine.drug
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 295
- Database :
- OpenAIRE
- Journal :
- Biochemical and Biophysical Research Communications
- Accession number :
- edsair.doi.dedup.....731bc68be79b268fac9cb0655c46748b