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          Institute: MPI für bioanorganische Chemie     Collection: MPI für bioanorganische Chemie     Display Documents



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ID: 733995.0, MPI für bioanorganische Chemie / MPI für bioanorganische Chemie
Direct Observation of an Iron-Bound Terminal Hydride in [FeFe]-Hydrogenase by Nuclear Resonance Vibrational Spectroscopy
Authors:Reijerse, Edward J.; Pham, Cindy C.; Pelmenschikov, Vladimir; Gilbert-Wilson, Ryan; Adamska-Venkatesh, Agnieszka; Siebel, Judith F.; Gee, Leland B.; Yoda, Yoshitaka; Tamasaku, Kenji; Lubitz, Wolfgang; Rauchfuss, Thomas B.; Cramer, Stephen P.
Language:English
Date of Publication (YYYY-MM-DD):2017
Title of Journal:Journal of the American Chemical Society
Journal Abbrev.:J.Am.Chem.Soc.
Volume:139
Issue / Number:12
Start Page:4306
End Page:4309
Review Status:Internal review
Audience:Experts Only
Abstract / Description:[FeFe]-hydrogenases catalyze the reversible reduction of protons to molecular hydrogen with extremely high efficiency. The active site ("H-cluster") consists of a [4Fe-4S]H cluster linked through a bridging cysteine to a [2Fe]H subsite coordinated by CN- and CO ligands featuring a dithiol-amine moiety that serves as proton shuttle between the protein proton channel and the catalytic distal iron site (Fed). Although there is broad consensus that an iron-bound terminal hydride species must occur in the catalytic mechanism, such a species has never been directly observed experimentally. Here, we present FTIR and nuclear resonance vibrational spectroscopy (NRVS) experiments in conjunction with density functional theory (DFT) calculations on an [FeFe]-hydrogenase variant lacking the amine proton shuttle which is stabilizing a putative hydride state. The NRVS spectra unequivocally show the bending modes of the terminal Fe H species fully consistent with widely accepted models of the catalytic cycle.
Comment of the Author/Creator:Date: 2017, MAR 29 2017
External Publication Status:published
Document Type:Article
Version Comment:Automatic journal name synchronization
Communicated by:N. N.
Affiliations:MPI für bioanorganische Chemie
Identifiers:ISI:000398247100018 [ID No:1]
ISSN:0002-7863 [ID No:2]
DOI:10.1021/jacs.7b00686 [ID No:3]
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