The spatio-temporal reduction and oxidation of protein thiols is an essential mechanism in signal transduction in all kingdoms of life. Thioredoxin (Trx) family proteins efficiently catalyse thiol-disulphide exchange reactions and the proteins are widely recognised for their importance in the operation of thiol switches. Trx family proteins have a broad and at the same time very distinct substrate specificity – a prerequisite for redox switching. Our research focuses on the following three points: (1.) the identification of physiologically or pathologically important redox switches in key proteins, (2.) the mechanisms of oxidation and reduction and how these control the proteins’ biological activity, and (3.) the molecular basis for the substrate and reaction specificity of Trx family proteins.

For further details, see: http://www.lillig.de

References

• Berndt C, Lillig CH. Glutathione, Glutaredoxins, and Iron. Antioxid Redox Signal. 2017;27: 1235-1251.
• Gellert, M., Hanschmann, E.M., Lepka, K., Berndt, C., and Lillig, C.H. Redox regulation of cytoskeletal dynamics during differentiation and de-differentiation. Biochim. Biophys. Acta - Gen. Sub. 2015;1850:1575-1587.
• Berndt, C., Lillig, C.H., Flohe , L. Redox regulation by glutathione needs enzymes. Front. Pharmacol. 2014;5:168.
• Hanschmann, E.M., Godoy, J.R., Berndt, C., Hudemann, C., and Lillig, C.H. Thioredoxins, glutaredoxins, and peroxiredoxins - molecular mechanisms and health significance: from cofactors to antioxidants to redox signaling. Antioxid. Redox Signal. 2013;19:1539-1605.