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Structural and spectroscopic characterization of a HdrA-like subunit from Hyphomicrobium denitrificans

2021-03Artigo científico Acesso aberto
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dc.contributor.authorErnst, Corvin
dc.contributor.authorKayastha, Kanwal
dc.contributor.authorKoch, Tobias
dc.contributor.authorVenceslau, Sofia S.
dc.contributor.authorPereira, Inês A.C.
dc.contributor.authorDemmer, Ulrike
dc.contributor.authorErmler, Ulrich
dc.contributor.authorDahl, Christiane
dc.contributor.institutionInstituto de Tecnologia Química e Biológica António Xavier (ITQB)
dc.contributor.pblFederation of European Biochemical Societies | Wiley
dc.date.accessioned2021-07-09T22:17:55Z
dc.date.available2021-07-09T22:17:55Z
dc.date.issued2021-03
dc.descriptionFunding Information: We thank Laurenz Heidrich for help with statistical analyses. This work was supported by grant Da 351/8‐1 (to CD) from the Deutsche Forschungsgemeinschaft and Fundação para a Ciência e Tecnologia (Portugal) (grant PTDC/BIA‐BQM/29118 and R&D units MOSTMICRO‐ITQB (UIDB/04612/2020 and UIDP/04612/2020), and European Union's Horizon 2020 research and innovation program (grant agreement No 810856). Open access funding enabled and organized by Projekt DEAL. Publisher Copyright: © 2020 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies Copyright: Copyright 2021 Elsevier B.V., All rights reserved.
dc.description.abstractMany bacteria and archaea employ a novel pathway of sulfur oxidation involving an enzyme complex that is related to the heterodisulfide reductase (Hdr or HdrABC) of methanogens. As a first step in the biochemical characterization of Hdr-like proteins from sulfur oxidizers (sHdr), we structurally analyzed the recombinant sHdrA protein from the Alphaproteobacterium Hyphomicrobium denitrificans at 1.4 Å resolution. The sHdrA core structure is similar to that of methanogenic HdrA (mHdrA) which binds the electron-bifurcating flavin adenine dinucleotide (FAD), the heart of the HdrABC-[NiFe]-hydrogenase catalyzed reaction. Each sHdrA homodimer carries two FADs and two [4Fe–4S] clusters being linked by electron conductivity. Redox titrations monitored by electron paramagnetic resonance and visible spectroscopy revealed a redox potential between −203 and −188 mV for the [4Fe–4S] center. The potentials for the FADH•/FADH− and FAD/FADH• pairs reside between −174 and −156 mV and between −81 and −19 mV, respectively. The resulting stable semiquinone FADH• species already detectable in the visible and electron paramagnetic resonance spectra of the as-isolated state of sHdrA is incompatible with basic principles of flavin-based electron bifurcation such that the sHdr complex does not apply this new mode of energy coupling. The inverted one-electron FAD redox potentials of sHdr and mHdr are clearly reflected in the different FAD-polypeptide interactions. According to this finding and the assumption that the sHdr complex forms an asymmetric HdrAA′B1C1B2C2 hexamer, we tentatively propose a mechanism that links protein-bound sulfane oxidation to sulfite on HdrB1 with NAD+ reduction via lipoamide disulfide reduction on HdrB2. The FAD of HdrA thereby serves as an electron storage unit. Database: Structural data are available in PDB database under the accession number 6TJR.en
dc.description.versionpublished
dc.format.extent15
dc.format.extent1995658
dc.identifier.doi10.1111/febs.15505
dc.identifier.issn1742-464X
dc.identifier.otherPURE: 32440692
dc.identifier.otherPURE UUID: c18f51e8-1ef3-4605-a495-6fe79793c668
dc.identifier.otherScopus: 85089506899
dc.identifier.otherPubMed: 32750208
dc.identifier.urihttp://hdl.handle.net/10362/120787
dc.identifier.urlhttps://www.scopus.com/pages/publications/85089506899
dc.language.isoeng
dc.peerreviewedyes
dc.subjectdissimilatory sulfur oxidation
dc.subjectelectron bifurcation
dc.subjectheterodisulfide reductase
dc.subjectHyphomicrobium denitrificans
dc.subjectBiochemistry
dc.subjectMolecular Biology
dc.subjectCell Biology
dc.titleStructural and spectroscopic characterization of a HdrA-like subunit from Hyphomicrobium denitrificansen
dc.typejournal article
degois.publication.firstPage1664
degois.publication.issue5
degois.publication.lastPage1678
degois.publication.titleFEBS Journal
degois.publication.volume288
dspace.entity.typePublication
rcaap.rightsopenAccess

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