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From chemRxiv
UC Irvine

Reducing CO2 to HCO2- at Mild Potentials: Lessons from Formate Dehydrogenase

The catalytic reduction of CO<sub>2</sub> to HCO<sub>2</sub><sup>-</sup> requires a formal transfer of a hydride (two electrons, one proton). Synthetic approaches for inorganic molecular catalysts have exclusively relied on classic metal hydrides, where the proton and electrons originate from the metal (via heterolytic cleavage of an M-H bond). An analysis of the scaling relationships that exist in classic metal hydrides reveal that hydride donors sufficiently hydridic to perform CO<sub>2</sub> reduction are only accessible at very reducing electrochemical potentials, which is consistent with known synthetic electrocatalysts. By comparison, the formate dehydrogenase enzymes operate at relatively mild potentials. In contrast to reported synthetic catalysts, none of the major mechanistic proposals for hydride transfer in formate dehydrogenase proceed through a classic metal hydride. Instead, they invoke formal hydride transfer from an orthogonal or bi-directional mechanism, where the proton and electron are not co-located. We discuss the thermodynamic advantages of this approach for favoring CO<sub>2</sub> reduction at mild potentials, along with guidelines for replicating this strategy in synthetic systems.
Published on July 16, 2020
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