You are here: Home :: Area NEM :: Life sciences :: Biochemistry

Alex Schneider, Wolfgang Brandt, Ludger A. Wessjohann

The influence of pH and flanking serine on the redox potential of S-S and SSe bridges of Cys-Cys and Cys-Sec peptides

Keywords: disulfides, Electrochemistry, selenenylsulfides, selenoproteins, thioredoxin reductase

In selenocysteine (Sec, U)-containing proteins the selenenylsulfide bridge and its reduced thiol-selenol counterpart are usually the significant species. An importance of serine as flanking amino acid on the redox potential of S-S and S-Se bridges was proposed for some thioredoxin reductases. To check the generality of this proposal, model tetrapeptides (GCCG, SCCG, GCCS, SCCS, GCUG, SCUG, GCUS, SCUS) were synthesized including the GCUG-sequence of human thioredoxin reductase. The influence on the redox potential of S-Se and S-S bridges in dependence of pH and of serine at different positions reveals (i) a strong general pHdependence, and (ii) a significant influence of flanking serine on disulfide only at basic pH.

Biological Chemistry, Walter de Gruyter

Print ISSN: 1431-6730
Volume: 2007
Pages: -

Show full article (external site)

Show all available items of this journal

 

Area NEM