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• W2149402746 abstract "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." @default.
• W2149402746 created "2016-06-24" @default.
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• W2149402746 date "2012-09-03" @default.
• W2149402746 modified "2023-10-18" @default.
• W2149402746 title "Revealing the Absolute Configuration of the CO and CN⁻Ligands at the Active Site of a [NiFe] Hydrogenase" @default.
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• W2149402746 doi "https://doi.org/10.1002/cphc.201200562" @default.
• W2149402746 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22945586" @default.
• W2149402746 hasPublicationYear "2012" @default.
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