{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Rodriguez-Macia P"],"funding":["Deutsche Forschungsgemeinschaft","Foundation for the National Institutes of Health","Einstein Stiftung Berlin","Max-Planck-Gesellschaft","NIGMS NIH HHS"],"pagination":["16786-16794"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7540559"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["59(38)"],"pubmed_abstract":["[FeFe] hydrogenases are the most active H<sub>2</sub> converting catalysts in nature, but their extreme oxygen sensitivity limits their use in technological applications. The [FeFe] hydrogenases from sulfate reducing bacteria can be purified in an O<sub>2</sub> -stable state called H<sub>inact</sub> . To date, the structure and mechanism of formation of H<sub>inact</sub> remain unknown. Our 1.65 Å crystal structure of this state reveals a sulfur ligand bound to the open coordination site. Furthermore, in-depth spectroscopic characterization by X-ray absorption spectroscopy (XAS), nuclear resonance vibrational spectroscopy (NRVS), resonance Raman (RR) spectroscopy and infrared (IR) spectroscopy, together with hybrid quantum mechanical and molecular mechanical (QM/MM) calculations, provide d"],"journal":["Angewandte Chemie (International ed. in English)"],"pubmed_title":["Caught in the H<sub>inact</sub> : Crystal Structure and Spectroscopy Reveal a Sulfur Bound to the Active Site of an O<sub>2</sub> -stable State of [FeFe] Hydrogenase."],"pmcid":["PMC7540559"],"funding_grant_id":["P41 GM103393","EVF-2016-277","EXC 2008 - 390540038","GM-65440","R01 GM065440","IS 1476/4-1","DE 1877/1-1","ZE 510/2-2","BI 2198/1-1"],"pubmed_authors":["Bjornsson R","DeBeer S","Zebger I","Birrell JA","Yoda Y","Lorent C","Span I","Cramer SP","Galle LM","Rodriguez-Macia P"],"additional_accession":[]},"is_claimable":false,"name":"Caught in the H<sub>inact</sub> : Crystal Structure and Spectroscopy Reveal a Sulfur Bound to the Active Site of an O<sub>2</sub> -stable State of [FeFe] Hydrogenase.","description":"[FeFe] hydrogenases are the most active H<sub>2</sub> converting catalysts in nature, but their extreme oxygen sensitivity limits their use in technological applications. The [FeFe] hydrogenases from sulfate reducing bacteria can be purified in an O<sub>2</sub> -stable state called H<sub>inact</sub> . To date, the structure and mechanism of formation of H<sub>inact</sub> remain unknown. Our 1.65 Å crystal structure of this state reveals a sulfur ligand bound to the open coordination site. Furthermore, in-depth spectroscopic characterization by X-ray absorption spectroscopy (XAS), nuclear resonance vibrational spectroscopy (NRVS), resonance Raman (RR) spectroscopy and infrared (IR) spectroscopy, together with hybrid quantum mechanical and molecular mechanical (QM/MM) calculations, provide d","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Sep","modification":"2026-05-02T22:49:58.501Z","creation":"2020-10-29T09:08:49Z"},"accession":"S-EPMC7540559","cross_references":{"pubmed":["32488975"],"doi":["10.1002/anie.202005208"]}}