[FeFe]-hydrogenases recieved increasing interest in the last decades. This review summarises important findings regarding their enzymatic reactivity as well as inorganic models applied as electro- and photochemical catalysts.

Electrochemical conversion of CO₂ to alcohols is one of the most challenging methods of conversion and storage of electrical energy in the form of high-energy fuels. The challenge lies in the catalyst design to enable its real-life implementation. Herein, we demonstrate the synthesis and characterization of a cobalt(III) triphenylphosphine corrole complex, which contains three polyethylene glycol residues attached at the meso-phenyl groups. Electron-donation and therefore reduction of the cobalt from cobalt(III) to cobalt(I) is accompanied by removal of the axial ligand, thus resulting in a square-planar cobalt(I) complex. The cobalt(I) as an electron-rich supernucleophilic d⁸-configurated metal centre, where two electrons occupy and fill up the antibonding d_z² orbital. This orbital possesses high affinity towards electrophiles, allowing for such electronically configurated metals reactions with carbon dioxide. Herein, we report the potential dependent heterogeneous electroreduction of CO₂ to ethanol or methanol of an immobilized cobalt A₃-corrole catalyst system. In moderately acidic aqueous medium (pH = 6.0), the cobalt corrole modified carbon paper electrode exhibits a Faradaic Efficiency (FE%) of 48 % towards ethanol production.

The need for sustainable catalysts for an efficient hydrogen evolution reaction is of significant interest for modern society. Inspired by comparable structural properties of [FeNi]-hydrogenase, here we present the natural ore pentlandite (Fe_4.5Ni_4.5S₈) as a direct ‘rock’ electrode material for hydrogen evolution under acidic conditions with an overpotential of 280 mV at 10 mA cm⁻². Furthermore, it reaches a value as low as 190 mV after 96 h of electrolysis due to surface sulfur depletion, which may change the electronic structure of the catalytically active nickel–iron centres. The ‘rock’ material shows an unexpected catalytic activity with comparable overpotential and Tafel slope to some well-developed metallic or nanostructured catalysts. Notably, the ‘rock’ material offers high current densities (≤650 mA cm⁻²) without any loss in activity for approximately 170 h. The superior hydrogen evolution performance of pentlandites as ‘rock’ electrode labels this ore as a promising electrocatalyst for future hydrogen-based economy.

Significance: The inability of CNS pathways to regenerate after injury can lead to devastating, life-long losses in sensory, motor, and other functions. We report that after injury to the optic nerve, a widely studied CNS pathway that normally cannot regenerate, mobile zinc (Zn ²⁺ ) increases rapidly in the processes of retinal interneurons (amacrine cells) and then transfers via vesicular release to retinal ganglion cells (RGCs), the injured projection neurons. Eliminating Zn ²⁺ leads to both persistent RGC survival and substantial axon regeneration with a broad therapeutic window. These findings show that signaling between interneurons and RGCs contributes to regulating the fate of RGCs after optic nerve injury, and that Zn ²⁺ chelation may provide a potent therapeutic approach.

[FeFe]-hydrogenases are nature's fastest catalysts for the evolution or oxidation of hydrogen. Numerous synthetic model complexes for the [2Fe] subcluster (2Fe_H) of their active site are known, but so far none of these could compete with the enzymes. The complex Fe₂[μ-(SCH₂)₂X](CN)₂(CO)₄ ²⁻ with X = NH was shown to integrate into the apo-form of [FeFe]-hydrogenases to yield a fully active enzyme. Here we report the first crystal structures of the apo-form of the bacterial [FeFe]-hydrogenase CpI from Clostridium pasteurianum at 1.60 Å and the active semisynthetic enzyme, CpI^ADT, at 1.63 Å. The structures illustrate the significant changes in ligand coordination upon integration and activation of the [2Fe] complex. These changes are induced by a rigid 2Fe_H cavity as revealed by the structure of apoCpI, which is remarkably similar to CpI^ADT. Additionally we present the high resolution crystal structures of the semisynthetic bacterial [FeFe]-hydrogenases CpI^PDT (X = CH₂), CpI^ODT (X = O) and CpI^SDT (X = S) with changes in the headgroup of the dithiolate bridge in the 2Fe_H cofactor. The structures of these inactive enzymes demonstrate that the 2Fe_H-subcluster and its protein environment remain largely unchanged when compared to the active enzyme CpI^ADT. As the active site shows an open coordination site in all structures, the absence of catalytic activity is probably not caused by steric obstruction. This demonstrates that the chemical properties of the dithiolate bridge are essential for enzyme activity.