scholarly journals Reversible Hydrogen Transfer Reactions in Thiyl Radicals From Cysteine and Related Molecules: Absolute Kinetics and Equilibrium Constants Determined by Pulse Radiolysis

2012 ◽  
Vol 116 (18) ◽  
pp. 5329-5341 ◽  
Author(s):  
Thomas Nauser ◽  
Willem H. Koppenol ◽  
Christian Schöneich

ChemInform ◽  
2014 ◽  
Vol 45 (23) ◽  
pp. no-no
Author(s):  
Christian Schoeneich ◽  
Olivier Mozziconacci ◽  
Willem H. Koppenol ◽  
Thomas Nauser


2014 ◽  
Vol 54 (3) ◽  
pp. 265-271 ◽  
Author(s):  
Christian Schöneich ◽  
Olivier Mozziconacci ◽  
Willem H. Koppenol ◽  
Thomas Nauser


2011 ◽  
Vol 39 (5) ◽  
pp. 1254-1259 ◽  
Author(s):  
Christian Schöneich

Cysteine thiyl radicals engage in reversible intramolecular hydrogen-transfer reactions with amino acid residues in peptides and proteins. These reactions can be experimentally demonstrated through covalent hydrogen–deuterium exchange when experiments are carried out in 2H2O. To this end, hydrogen-transfer reactions have been observed between cysteine thiyl radicals and glycine, alanine, serine, valine and leucine in both model peptides and a protein, insulin. The relevance of such reactions for protein oxidation under conditions of oxidative stress is discussed.









Sign in / Sign up

Export Citation Format

Share Document