%0 Journal Article
%A Caserta, Giorgio
%A Laun, Konstantin
%A Oudsen, Jean-Pierre
%A Sergueev, Ilya
%A Zebger, Ingo
%A Lenz, Oliver
%T NRVS Spectroscopy Resolves Distinct Bridging Hydride Intermediates in [NiFe]-Hydrogenase
%J Journal of the American Chemical Society
%V 147
%N 45
%@ 0002-7863
%C Washington, DC
%I ACS Publications
%M PUBDB-2025-04676
%P 41216 - 41220
%D 2025
%Z Open Access
%X The active-site iron of an H2-sensing [NiFe]-hydrogenase was selectively labeled with 57Fe, allowing the probing of all catalytic intermediates using synchrotron-based nuclear resonance vibrational spectroscopy. Diagnostic metal–hydride vibrations were detected for both the Nia-C and Nia-SR intermediates, with their assignments being confirmed through H/D isotope substitution and in situ hydride photolysis experiments. Interestingly, these Fe–hydride bands are separated by a large energy gap, reflecting distinct bonding interactions at the metal–hydride site. Despite these differences, vibrational analyses across all catalytically active species reveal a conserved structural rigidity of the [NiFe] center, which appears crucial for sustaining efficient and rapid electron transfer in [NiFe]-hydrogenases.
%F PUB:(DE-HGF)16
%9 Journal Article
%R 10.1021/jacs.5c15408
%U https://bib-pubdb1.desy.de/record/639802