- Ergebnisse als:
- Druckansicht
- Endnote (RIS)
- BibTeX
- Tabelle: CSV | HTML
Publikation
Publikation
Leitbild und Forschungsprofil
Molekulare Signalverarbeitung
Natur- und Wirkstoffchemie
Biochemie pflanzlicher Interaktionen
Stoffwechsel- und Zellbiologie
Unabhängige Nachwuchsgruppen
Program Center MetaCom
Publikationen
Gute Wissenschaftliche Praxis
Forschungsförderung
Netzwerke und Verbundprojekte
Symposien und Kolloquien
Alumni-Forschungsgruppen
Publikationen
Publikation
What makes selenoenzymes – seen from a chemist's view – so special that they cannot be substituted by just more analogous or adapted sulfur proteins? This review compiles and compares physicochemical properties of selenium and sulfur, synthetic routes to selenocysteine (Sec) and its peptides, and comparative studies of relevant thiols and selenols and their (mixed) dichalcogens, required to understand the special role of selenium in selenoproteins on the atomic molecular level. The biochemically most relevant differences are the higher polarizability of Se- and the lower pKa of SeH. The latter has a strikingly different pH-dependence than thiols, with selenols being active at much lower pH. Finally, selected typical enzymatic mechanisms which involve selenocysteine are critically discussed, also in view of the authors' own results.
Publikation
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.