Please use this identifier to cite or link to this item: http://dx.doi.org/10.14279/depositonce-5226
Main Title: Reductive activation and structural rearrangement in superoxide reductase: a combined infrared spectroscopic and computational study
Author(s): Horch, M.
Pinto, A. F.
Utesch, T.
Mroginski, M. A.
Romao, C. V.
Teixeira, M.
Hildebrandt, P.
Zebger, I.
Type: Article
Language Code: en
Abstract: Superoxide reductases (SOR) are a family of non-heme iron enzymes that limit oxidative stress by catalysing the reduction of superoxide to hydrogen peroxide and, thus, represent model systems for the detoxification of reactive oxygen species. In several enzymes of this type, reductive activation of the active site involves the reversible dissociation of a glutamate from the proposed substrate binding site at the iron. In this study we have employed IR spectroscopic and theoretical methods to gain insights into redox-linked structural changes of 1Fe-type superoxide reductases, focusing on the enzyme from the archaeon Ignicoccus hospitalis. Guided by crystal structure data and complemented by spectra calculation for an active site model, the main IR difference signals could be assigned. These signals reflect redox-induced structural changes in the first coordination sphere of the iron centre, adjacent loop and helical regions, and more remote β-sheets. By comparison with the spectra obtained for the E23A mutant of Ignicoccus hospitalis SOR, it is shown that glutamate E23 dissociates reversibly from the ferrous iron during reductive activation of the wild type enzyme. Moreover, this process is found to trigger a global conformational transition of the protein that is strictly dependent on the presence of E23. Similar concerted structural changes can be inferred from the IR spectra of related SORs such as that from Archaeoglobus fulgidus, indicating a widespread mechanism. A possible functional role of this process in terms of synergistic effects during reductive activation of the homotetrameric enzyme is proposed.
URI: http://depositonce.tu-berlin.de/handle/11303/5597
http://dx.doi.org/10.14279/depositonce-5226
Issue Date: 2014
Date Available: 22-Jun-2016
DDC Class: 540 Chemie und zugeordnete Wissenschaften
Sponsor/Funder: DFG, EXC 314, Unifying Concepts in Catalysis
Creative Commons License: https://creativecommons.org/licenses/by/3.0/
Journal Title: Physical chemistry, chemical physics
Publisher: Royal Society of Chemistry
Publisher Place: Cambridge
Volume: 16
Issue: 27
Publisher DOI: 10.1039/c4cp00884g
Page Start: 14220
Page End: 14230
EISSN: 1463-9076
Appears in Collections:Technische Universität Berlin » Fakultäten & Zentralinstitute » Fakultät 2 Mathematik und Naturwissenschaften » Institut für Chemie » Publications

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