Journal
CHEMBIOCHEM
Volume 23, Issue 14, Pages -Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.202200202
Keywords
bioinorganic chemistry; iron-sulfur clusters; metallopeptides; prebiotic chemistry; Rieske
Funding
- Simons Foundation [290358FY18, 290358FY19]
- Natural Sciences and Engineering Research Council of Canada (NSERC) [RGPIN-2020-04375]
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Iron-sulfur clusters are believed to be ancient cofactors that may have played a role in early protometabolic systems. This study investigates the properties of peptides containing cysteine and histidine ligands and their ability to coordinate [2Fe-2S] clusters, comparing them to purified iron-sulfur proteins. The findings suggest that these complexes may have been important for early cell-like systems.
Iron-sulfur clusters are thought to be ancient cofactors that could have played a role in early protometabolic systems. Thus far, redox active, prebiotically plausible iron-sulfur clusters have always contained cysteine ligands to the cluster. However, extant iron-sulfur proteins can be found to exploit other modes of binding, including ligation by histidine residues, as seen with [2Fe-2S] Rieske and MitoNEET proteins. Here, we investigated the ability of cysteine- and histidine-containing peptides to coordinate a mononuclear Fe2+ center and a [2Fe-2S] cluster and compare their properties with purified iron-sulfur proteins. The iron-sulfur peptides were characterized by UV-vis, circular dichroism, and paramagnetic NMR spectroscopies and cyclic voltammetry. Small (<= 6 amino acids) peptides can coordinate [2Fe-2S] clusters through a combination of cysteine and histidine residues with similar reduction potentials as their corresponding proteins. Such complexes may have been important for early cell-like systems.
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