Biochemical characterization of yeast mitochondrial Grx5 monothiol glutaredoxin.

doi:10.1074/jbc.M303477200

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Article

Biochemical characterization of yeast mitochondrial Grx5 monothiol glutaredoxin.

The Journal of biological chemistry - 11 Jul 2003

Tamarit Jordi, Belli Gemma, Cabiscol Elisa, Herrero Enrique, Ros Joaquim

Abstract excerpt

Grx5 is a yeast mitochondrial protein involved in iron-sulfur biogenesis that belongs to a recently described family of monothiolic glutaredoxin-like proteins. No member of this family has been biochemically characterized previously. Grx5 contains a conserved cysteine residue (Cys-60) and a non-conserved one (Cys-117). In this work, we have purified wild type and mutant C60S and C117S proteins and characterized...

Topics

Carbonic Anhydrases
Catalysis
Chromatography, High Pressure Liquid
Cysteine
Disulfides
Electrophysiology
Enzyme Inhibitors
Escherichia coli
Glutaredoxins
Glutathione
Glutathione Disulfide
Hydrogen-Ion Concentration
Iodoacetamide
Kinetics

Source

Open in PubMed

Identifiers

PMID: 12730244
DOI: 10.1074/jbc.M303477200

Provenance

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mitochondria

Models, Biological

Mutation

Oxidation-Reduction