Understanding the
[NiFe] Hydrogenase Active Site Environment
through Ultrafast Infrared and 2D-IR Spectroscopy of the Subsite Analogue
K[CpFe(CO)(CN)2] in Polar and Protic Solvents
posted on 2024-02-01, 20:13authored byBarbara Procacci, Solomon L. D. Wrathall, Amy L. Farmer, Daniel J. Shaw, Gregory M. Greetham, Anthony W. Parker, Yvonne Rippers, Marius Horch, Jason M. Lynam, Neil T. Hunt
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 H2O, D2O, 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.