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Influence of pH and flanking serine on the redox potential of S-S and S-Se bridges of Cys-Cys and Cys-Sec peptides

  • Alex Schneider , Wolfgang Brandt and Ludger A. Wessjohann
Published/Copyright: October 16, 2007
Biological Chemistry
From the journal Volume 388 Issue 10

Abstract

In selenocysteine (Sec, U)-containing proteins the selenenylsulfide bridge and its reduced thiol-selenol counterpart are usually the significant species. An important role for serine as flanking amino acid in 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 as a function of pH and of serine at different positions reveals (i) a strong general pH dependence, and (ii) a significant influence of flanking serine on disulfide only at basic pH.


Corresponding author

Received: 2007-4-30
Accepted: 2007-6-7
Published Online: 2007-10-16
Published in Print: 2007-10-01

©2007 by Walter de Gruyter Berlin New York

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