Exploring Structure and Function of Redox Intermediates in [NiFe]-Hydrogenases by an Advanced Experimental Approach for Solvated, Lyophilized and Crystallized Metalloenzymes

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dc.contributor.authorLorent, Christian
dc.contributor.authorPelmenschikov, Vladimir
dc.contributor.authorFrielingsdorf, Stefan
dc.contributor.authorSchoknecht, Janna
dc.contributor.authorCaserta, Giorgio
dc.contributor.authorYoda, Yoshitaka
dc.contributor.authorWang, Hongxin
dc.contributor.authorTamasaku, Kenji
dc.contributor.authorLenz, Oliver
dc.contributor.authorCramer, Stephen P.
dc.contributor.authorHorch, Marius
dc.contributor.authorLauterbach, Lars
dc.contributor.authorZebger, Ingo
dc.date.accessioned2022-12-29T09:25:58Z
dc.date.available2022-12-29T09:25:58Z
dc.date.issued2021-05-05
dc.description.abstractTo study metalloenzymes in detail, we developed a new experimental setup allowing the controlled preparation of catalytic intermediates for characterization by various spectroscopic techniques. The in situ monitoring of redox transitions by infrared spectroscopy in enzyme lyophilizate, crystals, and solution during gas exchange in a wide temperature range can be accomplished as well. Two O2-tolerant [NiFe]-hydrogenases were investigated as model systems. First, we utilized our platform to prepare highly concentrated hydrogenase lyophilizate in a paramagnetic state harboring a bridging hydride. This procedure proved beneficial for 57Fe nuclear resonance vibrational spectroscopy and revealed, in combination with density functional theory calculations, the vibrational fingerprint of this catalytic intermediate. The same in situ IR setup, combined with resonance Raman spectroscopy, provided detailed insights into the redox chemistry of enzyme crystals, underlining the general necessity to complement X-ray crystallographic data with spectroscopic analyses.en
dc.description.sponsorshipDFG, 390540038, EXC 2008: Unifying Systems in Catalysis "UniSysCat"
dc.description.sponsorshipDFG, 405325648, Engineering von O2-toleranten Hydrogenasen und ihre physiologischen Auswirkungen in rekombinanten Bakterien im Hinblick auf die Hydrogenase-abhängige NAD(P)H-Regeneration und H2-Produktion
dc.description.sponsorshipDFG, 311062227, Die Rolle von Eisen-Schwefel-Kofaktoren in der Assemblierung von Metallzentren und der Katalyse von Hydrogenasen
dc.description.sponsorshipEC/H2020/810856/EU/Twin to Illuminate Metals in Biology and Biocatalysis through Biospectroscopy/TIMB3
dc.description.sponsorshipTU Berlin, Open-Access-Mittel – 2021
dc.identifier.eissn1521-3757
dc.identifier.issn0044-8249
dc.identifier.urihttps://depositonce.tu-berlin.de/handle/11303/17909
dc.identifier.urihttps://doi.org/10.14279/depositonce-16698
dc.language.isoen
dc.relation.ispartof10.14279/depositonce-16579
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subject.ddc541 Physikalische Chemiede
dc.subject.other[NiFe]-hydrogenaseen
dc.subject.otherbiocatalysisen
dc.subject.otherin situ spectroscopyen
dc.subject.othermetalloenzymesen
dc.subject.othervibrational spectroscopyen
dc.titleExploring Structure and Function of Redox Intermediates in [NiFe]-Hydrogenases by an Advanced Experimental Approach for Solvated, Lyophilized and Crystallized Metalloenzymesen
dc.typeArticle
dc.type.versionpublishedVersion
dcterms.bibliographicCitation.doi10.1002/anie.202100451
dcterms.bibliographicCitation.issue29
dcterms.bibliographicCitation.journaltitleAngewandte Chemie
dcterms.bibliographicCitation.originalpublishernameWiley
dcterms.bibliographicCitation.originalpublisherplaceNew York, NY
dcterms.bibliographicCitation.pageend15862
dcterms.bibliographicCitation.pagestart15854
dcterms.bibliographicCitation.volume60
dcterms.rightsHolder.referenceCreative-Commons-Lizenz
tub.accessrights.dnbfree
tub.affiliationFak. 2 Mathematik und Naturwissenschaften::Inst. Chemie::FG Physikalische Chemie / Biophysikalische Chemie
tub.publisher.universityorinstitutionTechnische Universität Berlin

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