id,collection,dc.contributor.author,dc.date.accessioned,dc.date.available,dc.date.issued,dc.description.abstract[en],dc.format.extent,dc.identifier.uri,dc.language,dc.rights.uri,dc.subject.ddc,dc.subject[en],dc.title,dc.type,dcterms.accessRights.openaire,dcterms.bibliographicCitation.doi,dcterms.bibliographicCitation.journaltitle,dcterms.bibliographicCitation.number,dcterms.bibliographicCitation.pageend,dcterms.bibliographicCitation.pagestart,dcterms.bibliographicCitation.url,dcterms.bibliographicCitation.volume,dcterms.isPartOf.eissn,dcterms.isPartOf.issn,refubium.affiliation,refubium.affiliation.other,refubium.resourceType.isindependentpub "afba51c0-ede2-467e-b355-b04104f86921","fub188/16","Mebs, Stefan||Senger, Moritz||Duan, Jifu||Wittkamp, Florian||Apfel, Ulf-Peter||Happe, Thomas||Winkler, Martin||Stripp, Sven T.||Haumann, Michael","2019-10-29T14:18:46Z","2019-10-29T14:18:46Z","2017","[FeFe]-Hydrogenases contain a H2-converting cofactor (H-cluster) in which a canonical [4Fe–4S] cluster is linked to a unique diiron site with three carbon monoxide (CO) and two cyanide (CN–) ligands (e.g., in the oxidized state, Hox). There has been much debate whether reduction and hydrogen binding may result in alternative rotamer structures of the diiron site in a single (Hred) or double (Hsred) reduced H-cluster species. We employed infrared spectro-electrochemistry and site-selective isotope editing to monitor the CO/CN– stretching vibrations in [FeFe]-hydrogenase HYDA1 from Chlamydomonas reinhardtii. Density functional theory calculations yielded vibrational modes of the diatomic ligands for conceivable H-cluster structures. Correlation analysis of experimental and computational IR spectra has facilitated an assignment of Hred and Hsred to structures with a bridging hydride at the diiron site. Pronounced ligand rotation during μH binding seems to exclude Hred and Hsred as catalytic intermediates. Only states with a conservative H-cluster geometry featuring a μCO ligand are likely involved in rapid H2 turnover.","11 Seiten","https://refubium.fu-berlin.de/handle/fub188/25836||http://dx.doi.org/10.17169/refubium-25597","eng","http://www.fu-berlin.de/sites/refubium/rechtliches/Nutzungsbedingungen","500 Naturwissenschaften und Mathematik::540 Chemie::541 Physikalische Chemie","H-cluster||[FeFe]-hydrogenases||infrared spectroscopy","Bridging hydride at reduced H-cluster species in [FeFe]-hydrogenases revealed by infrared spectroscopy, isotope editing, and quantum chemistry","Wissenschaftlicher Artikel","open access","10.1021/jacs.7b07548","Journal of the American Chemical Society","35","12160","12157","https://doi.org/10.1021/jacs.7b07548","139","1520-5126","0002-7863","Physik","Institut für Experimentalphysik:::0e15dd66-95f1-40d5-8307-e68203f86a76:::600","no"