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| 001 | 639802 | ||
| 005 | 20251119161944.0 | ||
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| 100 | 1 | _ | |a Caserta, Giorgio |0 P:(DE-H253)PIP1092788 |b 0 |e Corresponding author |
| 245 | _ | _ | |a NRVS Spectroscopy Resolves Distinct Bridging Hydride Intermediates in [NiFe]-Hydrogenase |
| 260 | _ | _ | |a Washington, DC |c 2025 |b ACS Publications |
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| 520 | _ | _ | |a 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. |
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