Designing biomimetic materials with high activity and customized biological functions by
mimicking the central structure of biomolecules has become an important avenue for the …

Iron–sulfur clusters have been reported to catalyze various redox transformations, including
the multielectron reduction of CO2 to hydrocarbons. Herein, we report the design and …

Attempts to generate open coordination sites for N2 binding at synthetic Fe–S clusters often
instead result in cluster oligomerization. Recently, it was shown for Mo–Fe–S clusters that …

Oxidoreductases play crucial roles in electron transfer during biological redox reactions.
These reactions are not exclusive to protein-based biocatalysts; nano-size (< 100 nm), fine …

The iron–molybdenum cofactor of nitrogenase (FeMoco) catalyzes fixation of N2 via Fe
hydride intermediates. Our understanding of these species has relied heavily on the …

Biological multielectron reactions often are performed by metalloenzymes with
heterometallic sites, such as anaerobic carbon monoxide dehydrogenase (CODH), which …

Synthetic analogues of the three common types of Fe–S clusters found in biology─ diamond-
core [Fe2S2] clusters, open-cuboidal [Fe3S4] clusters, and cuboidal [Fe4S4] clusters─ have …

The FeMo cofactor (FeMoco) of Mo nitrogenase is responsible for reducing dinitrogen to
ammonia, but it requires the addition of 3–4 e–/H+ pairs before N2 even binds. A binding …

Cuboidal [Fe4S4] clusters are ubiquitous cofactors in biological redox chemistry. In the
[Fe4S4] 1+ state, pairwise spin coupling gives rise to six arrangements of the Fe valences …

Nitrogenases, the enzymes that convert N2 to NH3, also catalyze the reductive coupling of
CO to yield hydrocarbons. CO-coordinated species of nitrogenase clusters have been …