Spin Polarization Reveals the Coordination Geometry of the [FeFe] Hydrogenase Active Site in Its CO-Inhibited State

• Published in: The journal of physical chemistry letters Vol. 11; no. 12; pp. 4597 - 4602
• Main Authors: Reijerse, Edward, Birrell, James A, Lubitz, Wolfgang
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 18-06-2020
• Subjects: Algal Proteins - antagonists & inhibitors; Algal Proteins - chemistry; Bacterial Proteins - antagonists & inhibitors; Bacterial Proteins - chemistry; Carbon Isotopes - chemistry; Carbon Monoxide - chemistry; Catalytic Domain; Chlamydomonas reinhardtii - enzymology; Clostridium - enzymology; Coordination Complexes - chemistry; Density Functional Theory; Electron Spin Resonance Spectroscopy; Enzyme Inhibitors - chemistry; Hydrogenase - antagonists & inhibitors; Hydrogenase - chemistry; Iron - chemistry; Iron-Sulfur Proteins - antagonists & inhibitors; Iron-Sulfur Proteins - chemistry; Letter; Ligands; Models, Chemical; Molecular Structure
• ISSN: 1948-7185; 1948-7185
• DOI: 10.1021/acs.jpclett.0c01352

The active site of [FeFe] hydrogenase features a binuclear iron cofactor Fe
ADT(CO)
(CN)
, where ADT represents the bridging ligand aza-propane-dithiolate. The terminal diatomic ligands all coordinate in a basal configuration, and one CO bridges the two irons leaving an open coordination site at which the hydrogen species and the competitive inhibitor CO bind. Externally supplied CO is expected to coordinate in an apical configuration. However, an alternative configuration has been proposed in which, due to ligand rotation, the CN
bound to the distal Fe becomes apical. Using selective
C isotope labeling of the CN
and CO
ligands in combination with pulsed
C electron-nuclear-nuclear triple resonance spectroscopy, spin polarization effects are revealed that, according to density functional theory calculations, are consistent with only the "unrotated" apical CO
configuration.