Reductive activation and structural rearrangement in superoxide reductase: a combined infrared spectroscopic and computational study

Simple item page
dc.contributor.authorHorch, M.
dc.contributor.authorPinto, A. F.
dc.contributor.authorUtesch, T.
dc.contributor.authorMroginski, M. A.
dc.contributor.authorRomao, C. V.
dc.contributor.authorTeixeira, M.
dc.contributor.authorHildebrandt, P.
dc.contributor.authorZebger, I.
dc.date.accessioned2016-06-22T08:05:32Z
dc.date.available2016-06-22T08:05:32Z
dc.date.issued2014
dc.description.abstractSuperoxide 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.en
dc.description.sponsorshipDFG, EXC 314, Unifying Concepts in Catalysisen
dc.identifier.eissn1463-9076
dc.identifier.pmid24912395
dc.identifier.urihttps://depositonce.tu-berlin.de/handle/11303/5597
dc.identifier.urihttp://dx.doi.org/10.14279/depositonce-5226
dc.language.isoen
dc.rights.urihttps://creativecommons.org/licenses/by/3.0/
dc.subject.ddc540 Chemie und zugeordnete Wissenschaftende
dc.titleReductive activation and structural rearrangement in superoxide reductase: a combined infrared spectroscopic and computational studyen
dc.typeArticleen
dc.type.versionpublishedVersionen
dcterms.bibliographicCitation.doi10.1039/c4cp00884g
dcterms.bibliographicCitation.issue27
dcterms.bibliographicCitation.journaltitlePhysical chemistry, chemical physicsen
dcterms.bibliographicCitation.originalpublishernameRoyal Society of Chemistryde
dcterms.bibliographicCitation.originalpublisherplaceCambridgede
dcterms.bibliographicCitation.pageend14230
dcterms.bibliographicCitation.pagestart14220
dcterms.bibliographicCitation.volume16
tub.accessrights.dnbfree
tub.affiliationFak. 2 Mathematik und Naturwissenschaften::Inst. Chemiede
tub.affiliation.facultyFak. 2 Mathematik und Naturwissenschaftende
tub.affiliation.instituteInst. Chemiede
tub.publisher.universityorinstitutionTechnische Universität Berlin

Files

Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
c4cp00884g.pdf
Size:
4.06 MB
Format:
Adobe Portable Document Format
Download

Collections

Publications