Skip to main content
Article thumbnail
Location of Repository

Metal-induced histidine deprotonation in biocatalysis? Experimental and theoretical insights into superoxide reductase

By Marius Horch, Ana Filipa Pinto, Maria Andrea Mroginski, Miguel Teixeira, Peter Hildebrandt and Ingo Zebger

Abstract

Metal-induced histidine deprotonation may have tremendous effects on metalloprotein catalysis. Here, we explore protonation states of all active site histidines in superoxide reductase (SOR), a non-heme iron enzyme catalysing the reduction of superoxide to hydrogen peroxide. Using experimental and theoretical techniques, we show that these amino acids remain in their neutral state under physiological conditions, excluding deprotonation. Based on our findings, alternative explanations for lack of H/D exchange of SOR histidines are discussed, including high barriers for acid/base reactions of coordinated ligands

Topics: 540 Chemie und zugeordnete Wissenschaften
Year: 2014
DOI identifier: 10.1039/c4ra11976b
OAI identifier: oai:depositonce.tu-berlin.de:11303/5573
Provided by: DepositOnce
Journal:
Download PDF:
Sorry, we are unable to provide the full text but you may find it at the following location(s):
  • https://creativecommons.org/li... (external link)
  • http://dx.doi.org/10.14279/dep... (external link)
  • http://depositonce.tu-berlin.d... (external link)
  • Suggested articles


    To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.