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Revealing the absolute configuration of the CO and CN- ligands at the active site of a [NiFe] hydrogenase

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Published copy (DOI)

Author(s)

  • Yvonne Rippers
  • Marius Horch
  • Peter Hildebrandt
  • Ingo Zebger
  • Maria Andrea Mroginski

Department/unit(s)

Publication details

JournalChemPhysChem
DatePublished - 7 Dec 2012
Issue number17
Volume13
Number of pages5
Pages (from-to)3852-3856
Original languageEnglish

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.

    Research areas

  • configuration determination, hydrogenase, IR spectroscopy, metalloenzymes, molecular modeling

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