| Autor: |
Procacci B; Department of Chemistry, York Biomedical Research Institute, University of York, York YO10 5DD, U.K., Wrathall SLD; Department of Chemistry, York Biomedical Research Institute, University of York, York YO10 5DD, U.K., Farmer AL; Department of Chemistry, York Biomedical Research Institute, University of York, York YO10 5DD, U.K., Shaw DJ; Department of Chemistry, York Biomedical Research Institute, University of York, York YO10 5DD, U.K., Greetham GM; STFC Central Laser Facility, Research Complex at Harwell, Rutherford Appleton Laboratory, Harwell Campus, Didcot OX11 0QX, U.K., Parker AW; STFC Central Laser Facility, Research Complex at Harwell, Rutherford Appleton Laboratory, Harwell Campus, Didcot OX11 0QX, U.K., Rippers Y; Department of Physics, Ultrafast Dynamics in Catalysis, Freie Universität Berlin, Arnimallee 14, 14195 Berlin, Germany., Horch M; Department of Physics, Ultrafast Dynamics in Catalysis, Freie Universität Berlin, Arnimallee 14, 14195 Berlin, Germany., Lynam JM; Department of Chemistry, York Biomedical Research Institute, University of York, York YO10 5DD, U.K., Hunt NT; Department of Chemistry, York Biomedical Research Institute, University of York, York YO10 5DD, U.K. |
| Abstrakt: |
The [CpFe(CO)(CN) 2 ] - unit is an excellent structural model for the Fe(CO)(CN) 2 moiety of the active site found in [NiFe] hydrogenases. Ultrafast infrared (IR) pump-probe and 2D-IR spectroscopy have been used to study K[CpFe(CO)(CN) 2 ] ( M1 ) in a range of protic and polar solvents and as a dry film. Measurements of anharmonicity, intermode vibrational coupling strength, vibrational relaxation time, and solvation dynamics of the CO and CN stretching modes of M1 in H 2 O, D 2 O, methanol, dimethyl sulfoxide, and acetonitrile reveal that H-bonding to the CN ligands plays an important role in defining the spectroscopic characteristics and relaxation dynamics of the Fe(CO)(CN) 2 unit. Comparisons of the spectroscopic and dynamic data obtained for M1 in solution and in a dry film with those obtained for the enzyme led to the conclusion that the protein backbone forms an important part of the bimetallic active site environment via secondary coordination sphere interactions. |
