Please use this identifier to cite or link to this item: http://dx.doi.org/10.14279/depositonce-5202
Main Title: Metal-induced histidine deprotonation in biocatalysis? Experimental and theoretical insights into superoxide reductase
Author(s): Horch, Marius
Pinto, Ana Filipa
Mroginski, Maria Andrea
Teixeira, Miguel
Hildebrandt, Peter
Zebger, Ingo
Type: Article
Language Code: en
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.
URI: http://depositonce.tu-berlin.de/handle/11303/5573
http://dx.doi.org/10.14279/depositonce-5202
Issue Date: 2014
Date Available: 21-Jun-2016
DDC Class: 540 Chemie und zugeordnete Wissenschaften
Creative Commons License: https://creativecommons.org/licenses/by/3.0/
Journal Title: RSC Advances : an international journal to further the chemical sciences
Publisher: Royal Society of Chemistry
Publisher Place: Cambridge
Volume: 4
Issue: 96
Publisher DOI: 10.1039/c4ra11976b
Page Start: 54091
Page End: 54095
EISSN: 2046-2069
Appears in Collections:Technische Universität Berlin » Fakultäten & Zentralinstitute » Fakultät 2 Mathematik und Naturwissenschaften » Institut für Chemie » Publications

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