Natural products have been extensively applied in clinical practice, characterized by multi-
component and multi-target, many pharmacodynamic substances, complex action …

The comparison of homologous metalloenzymes, in which the same inorganic active site is
surrounded by a variable protein matrix, has demonstrated that residues that are remote …

Synthetic [Fe4S4] clusters with Fe–R groups (R= alkyl/benzyl) are shown to release organic
radicals on an [Fe4S4] 3+–R/[Fe4S4] 2+ redox couple, the same that has been proposed for …

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 …

[FeFe]-hydrogenases catalyze the reversible oxidation of H 2 from electrons and protons at
an organometallic active site cofactor named the H-cluster. In addition to the H-cluster, most …

Electron bifurcation is an elegant mechanism of biological energy conversion that effectively
couples three different physiologically relevant substrates. As such, enzymes that perform …

Ferredoxins (Fds) are small proteins which shuttle electrons to pathways like biological
nitrogen fixation. Physical properties tune the reactivity of Fds with different pathways, but …

Fe-S clusters are ubiquitous inorganic cofactors found in proteins across all domains of life,
including viruses. Their prevalence stems from their unique redox and structural plasticity …

Hydrogenases are a diverse group of metalloenzymes that catalyze the conversion of H 2
into protons and electrons and the reverse reaction. A subgroup is formed by the [FeFe] …

To investigate the effect of long‐distance organic ligand on electronic coupling between
metallic atoms, the mononuclear and dinuclear complexes [Cp (dppe) Fe (apc)](1),[{Cp …