Simulation of electrocatalytic hydrogen production by a bioinspired catalyst anchored to a pyrite electrode.
The possibility of using the active site, the [FeFe](H) cluster, of the bacterial di-iron hydrogenases as a catalyst for hydrogen production from water by electro- or photocatalysis is of current scientific and technological interest. We present here a theoretical study of hydrogen production by a modified [FeFe](H) cluster stably linked to a pyrite electrode immersed in acidified water. We employed state-of-the-art electronic-structure and first-principles molecular-dynamics methods. We found that a stable sulfur link of the cluster to the surface analogous to that linking the cluster to its enzyme environment cannot be made. However, we have discovered a modification of the cluster which does form a stable, tridentate link to the surface. The pyrite electrode readily produces hydrogen from acidified water when functionalized with the modified cluster, which remains stable throughout the hydrogen production cycle.
Zipoli
Federico
F
Department of Chemistry, Princeton University, Princeton, New Jersey 08544, USA. fzipoli@princeton.edu
Car
Roberto
R
Cohen
Morrel H
MH
Selloni
Annabella
A
D032701:Biomimetics; D002384:Catalysis; D020134:Catalytic Domain; D004563:Electrochemistry; D004566:Electrodes; D006859:Hydrogen / Q000737:chemistry*; D006864:Hydrogenase / Q000737:chemistry / Q000378:metabolism; D007501:Iron / Q000737:chemistry*; D007506:Iron-Sulfur Proteins / Q000737:chemistry / Q000378:metabolism; D056004:Molecular Dynamics Simulation; D010084:Oxidation-Reduction; D011522:Protons; D013440:Sulfides / Q000737:chemistry*; D013499:Surface Properties; D014867:Water / Q000737:chemistry
D007506:Iron-Sulfur Proteins; D011522:Protons; D013440:Sulfides; D014867:Water; C011342:pyrite; D006859:Hydrogen; D007501:Iron; C118830:iron hydrogenase; D006864:Hydrogenase