Login / Signup

Time-Resolved Infrared Spectroscopy Reveals the pH-Independence of the First Electron Transfer Step in the [FeFe] Hydrogenase Catalytic Cycle.

Monica L K SanchezSeth WileyEdward J ReijerseWolfgang LubitzJames A BirrellR Brian Dyer
Published in: The journal of physical chemistry letters (2022)
[FeFe] hydrogenases are highly active catalysts for hydrogen conversion. Their active site has two components: a [4Fe-4S] electron relay covalently attached to the H 2 binding site and a diiron cluster ligated by CO, CN - , and 2-azapropane-1,3-dithiolate (ADT) ligands. Reduction of the [4Fe-4S] site was proposed to be coupled with protonation of one of its cysteine ligands. Here, we used time-resolved infrared (TRIR) spectroscopy on the [FeFe] hydrogenase from Chlamydomonas reinhardtii ( Cr HydA1) containing a propane-1,3-dithiolate (PDT) ligand instead of the native ADT ligand. The PDT modification does not affect the electron transfer step to [4Fe-4S] H but prevents the enzyme from proceeding further through the catalytic cycle. We show that the rate of the first electron transfer step is independent of the pH, supporting a simple electron transfer rather than a proton-coupled event. These results have important implications for our understanding of the catalytic mechanism of [FeFe] hydrogenases and highlight the utility of TRIR.
Keyphrases
  • electron transfer
  • photodynamic therapy
  • metal organic framework
  • crystal structure
  • high resolution
  • single molecule
  • mouse model
  • lymph node metastasis
  • mass spectrometry
  • living cells