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Glutaredoxins that contain a Cys-X-X-Cys active site motif are glutathione-dependent thiol-disulfide oxidoreductases. Vertebrate glutaredoxin 2 is characterized by two extra cysteines that form an intra-molecular disulfide bridge. Zebrafish glutaredoxin 2 contains four additional cysteines that are conserved within the infraclass of bony fish (teleosts). Here, we present a biochemical and biophysical characterization of zebrafish glutaredoxin 2, focusing on iron-sulfur-cluster coordination. The coordination of [2Fe2S](2+)-clusters in monomers of this protein was revealed by both absorption and Mössbauer spectroscopy as well as size exclusion chromatography. All other holo-glutaredoxins represent [FeS]-cluster bridged dimers using two molecules of non-covalently bound glutathione and the N-terminal active site cysteines as ligands. These cysteine residues were not required for [FeS]-cluster coordination in zebrafish glutaredoxin 2. A crystal structure of the teleost protein revealed high structural similarity to its human homologue. The two vertebrate-specific cysteines as well as two of the teleost-specific cysteines are positioned within a radius of 7Å near the C-terminus suggesting a potential role in [FeS]-cluster coordination. Indeed, mutated proteins lacking these teleost-specific cysteines lost the ability to bind the cofactor. Hence, the apparent mode of [FeS]-cluster coordination in zebrafish glutaredoxin 2 could be different from all yet described [FeS]-glutaredoxins.

Original publication




Journal article


Biochem biophys res commun

Publication Date





491 - 496


Crystal structure, GSH, GSSG, Glutathione, Grx, HED, Mössbauer spectroscopy, Redox, Trx, Zebrafish, glutaredoxin, glutathion, glutathione disulphide, hydroxyethyl disulphide, thioredoxin, Amino Acid Motifs, Animals, Catalytic Domain, Cysteine, Enzyme Activation, Glutaredoxins, Humans, Iron-Sulfur Proteins, Ligands, Molecular Sequence Data, Protein Binding, Protein Multimerization, Sequence Homology, Amino Acid, Zebrafish, Zebrafish Proteins