Spontaneous assembly of redox-active iron-sulfur clusters at low concentrations of cysteine

This is the authors' abstract. We don't add key points for this paper.

Iron-sulfur (FeS) proteins are ancient and fundamental to life, being involved in electron transfer and CO 2 fixation. FeS clusters have structures similar to the unit-cell of FeS minerals such as greigite, found in hydrothermal systems linked with the origin of life. However, the prebiotic pathway from mineral surfaces to biological clusters is unknown. Here we show that FeS clusters form spontaneously through interactions of inorganic Fe 2+ /Fe 3+ and S 2− with micromolar concentrations of the amino acid cysteine in water at alkaline pH. Bicarbonate ions stabilize the clusters and even promote cluster formation alone at concentrations >10 mM, probably through salting-out effects. We demonstrate robust, concentration-dependent formation of [4Fe4S], [2Fe2S] and mononuclear iron clusters using UV-Vis spectroscopy, 57 Fe-Mössbauer spectroscopy and 1 H-NMR. Cyclic voltammetry shows that the clusters are redox-active. Our findings reveal that the structures responsible for biological electron transfer and CO 2 reduction could have formed spontaneously from monomers at the origin of life.