Light-Driven Hydrogen Evolution Reaction Catalyzed by a Molybdenum–Copper Artificial Hydrogenase

Orange protein (Orp) is a small bacterial metalloprotein of unknown function that harbors a unique molybdenum/copper (Mo/Cu) heterometallic cluster, [S₂MoS₂CuS₂MoS₂]^3-. In this paper, the performance of Orp as a catalyst for the photocatalytic reduction of protons into H₂ has been investigated under visible light irradiation. We report the complete biochemical and spectroscopic characterization of holo-Orp containing the [S₂MoS₂CuS₂MoS₂]^3- cluster, with docking and molecular dynamics simulations suggesting a positively charged Arg, Lys-containing pocket as the binding site. Holo-Orp exhibits excellent photocatalytic activity, in the presence of ascorbate as the sacrificial electron donor and [Ru(bpy)₃]Cl₂ as the photosensitizer, for hydrogen evolution with a maximum turnover number of 890 after 4 h irradiation. Density functional theory (DFT) calculations were used to propose a consistent reaction mechanism in which the terminal sulfur atoms are playing a key role in promoting H₂ formation. A series of dinuclear [S₂MS₂M'S₂MS₂]^(4n)- clusters, with M = Mo^VI, W^VI and M'⁽ⁿ⁺⁾ = Cu^I, Fe^I, Ni^I, Co^I, Zn^II, Cd^II were assembled in Orp, leading to different M/M'-Orp versions which are shown to display catalytic activity, with the Mo/Fe-Orp catalyst giving a remarkable turnover number (TON) of 1150 after 2.5 h reaction and an initial turnover frequency (TOF°) of 800 h^-1 establishing a record among previously reported artificial hydrogenases.