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000639802 1001_ $$0P:(DE-H253)PIP1092788$$aCaserta, Giorgio$$b0$$eCorresponding author
000639802 245__ $$aNRVS Spectroscopy Resolves Distinct Bridging Hydride Intermediates in [NiFe]-Hydrogenase
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000639802 520__ $$aThe 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.
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