{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Rohac R"],"funding":["Agence Nationale de la Recherche","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["8499-8508"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8300475"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["143(22)"],"pubmed_abstract":["[FeFe]-hydrogenases use a unique organometallic complex, termed the H cluster, to reversibly convert H<sub>2</sub> into protons and low-potential electrons. It can be best described as a [Fe<sub>4</sub>S<sub>4</sub>] cluster coupled to a unique [2Fe]<sub>H</sub> center where the reaction actually takes place. The latter corresponds to two iron atoms, each of which is bound by one CN<sup>-</sup> ligand and one CO ligand. The two iron atoms are connected by a unique azadithiolate molecule (<sup>-</sup>S-CH<sub>2</sub>-NH-CH<sub>2</sub>-S<sup>-</sup>) and an additional bridging CO. This [2Fe]<sub>H</sub> center is built stepwise thanks to the well-orchestrated action of maturating enzymes that belong to the Hyd machinery. Among them, HydG converts l-tyrosine into CO and CN<sup>-</sup> to produce a unique l-cysteine-Fe(CO)<sub>2</sub>CN species termed complex-B. Very recently, HydE was shown to perform radical-based chemistry using synthetic complex-B as a substrate. Here we report the high-resolution crystal structure that establishes the identity of the complex-B-bound HydE. By triggering the reaction prior to crystallization, we trapped a new five-coordinate Fe species, supporting the proposal that HydE performs complex modifications of complex-B to produce a monomeric \"SFe(CO)<sub>2</sub>CN\" precursor to the [2Fe]<sub>H</sub> center. Substrate access, product release, and intermediate transfer are also discussed."],"journal":["Journal of the American Chemical Society"],"pubmed_title":["Crystal Structure of the [FeFe]-Hydrogenase Maturase HydE Bound to Complex-B."],"pmcid":["PMC8300475"],"funding_grant_id":["GM-61153","1R35GM126961","R35 GM126961","R01 GM061153","ANR-17-EURE-0003","ANR-15-IDEX-02","ANR-10-INBS-05-02"],"pubmed_authors":["Britt RD","Tao L","Martin L","Liu L","Nicolet Y","Rauchfuss TB","Basu D","Rohac R"],"additional_accession":[]},"is_claimable":false,"name":"Crystal Structure of the [FeFe]-Hydrogenase Maturase HydE Bound to Complex-B.","description":"[FeFe]-hydrogenases use a unique organometallic complex, termed the H cluster, to reversibly convert H<sub>2</sub> into protons and low-potential electrons. It can be best described as a [Fe<sub>4</sub>S<sub>4</sub>] cluster coupled to a unique [2Fe]<sub>H</sub> center where the reaction actually takes place. The latter corresponds to two iron atoms, each of which is bound by one CN<sup>-</sup> ligand and one CO ligand. The two iron atoms are connected by a unique azadithiolate molecule (<sup>-</sup>S-CH<sub>2</sub>-NH-CH<sub>2</sub>-S<sup>-</sup>) and an additional bridging CO. This [2Fe]<sub>H</sub> center is built stepwise thanks to the well-orchestrated action of maturating enzymes that belong to the Hyd machinery. Among them, HydG converts l-tyrosine into CO and CN<sup>-</sup> to produce a unique l-cysteine-Fe(CO)<sub>2</sub>CN species termed complex-B. Very recently, HydE was shown to perform radical-based chemistry using synthetic complex-B as a substrate. Here we report the high-resolution crystal structure that establishes the identity of the complex-B-bound HydE. By triggering the reaction prior to crystallization, we trapped a new five-coordinate Fe species, supporting the proposal that HydE performs complex modifications of complex-B to produce a monomeric \"SFe(CO)<sub>2</sub>CN\" precursor to the [2Fe]<sub>H</sub> center. Substrate access, product release, and intermediate transfer are also discussed.","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Jun","modification":"2026-05-31T07:02:50.337Z","creation":"2025-02-18T23:32:40.772Z"},"accession":"S-EPMC8300475","cross_references":{"pubmed":["34048236"],"doi":["10.1021/jacs.1c03367"]}}