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Revealing the Absolute Configuration of the CO and CN- Ligands at the Active Site of a [NiFe] Hydrogenase
Citation key Rippers2012
Author Rippers, Yvonne and Horch, Marius and Hildebrandt, Peter and Zebger, Ingo and Mroginski, Maria Andrea
Pages 3852–3856
Year 2012
DOI 10.1002/cphc.201200562
Journal Chemphyschem
Volume 13
Number 17
Month dec
Abstract Combined molecular dynamics (MD) and quantum mechanical/molecular mechanical (QM/MM) calculations were performed on the crystal structure of the reduced membrane-bound [NiFe] hydrogenase (MBH) from Ralstonia eutropha to determine the absolute configuration of the CO and the two CN- ligands bound to the active-site iron of the enzyme. For three models that include the CO ligand at different positions, often indistinguishable on the basis of the crystallographic data, we optimized the structures and calculated the ligand stretching frequencies. Comparison with the experimental IR data reveals that the CO ligand is in trans position to the substrate-binding site of the bimetallic [NiFe] cluster.
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