Understanding the structure and dynamics of hydrogenases by ultrafast and two-dimensional infrared spectroscopy.

ABSTRACT: Hydrogenases are valuable model enzymes for sustainable energy conversion approaches using H₂, but rational utilization of these base-metal biocatalysts requires a detailed understanding of the structure and dynamics of their complex active sites. The intrinsic CO and CN^- ligands of these metalloenzymes represent ideal chromophores for infrared (IR) spectroscopy, but structural and dynamic insight from conventional IR absorption experiments is limited. Here, we apply ultrafast and two-dimensional (2D) IR spectroscopic techniques, for the first time, to study hydrogenases in detail. Using an O₂-tolerant [NiFe] hydrogenase as a model system, we demonstrate that IR pump-probe spectroscopy can explore catalytically relevant ligand bonding by accessing high-lyin

SUBMITTER: Horch M 

PROVIDER: S-EPMC6857670 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature