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.

Histidine Ligated Iron-Sulfur Peptides / Valer, Luca; Rossetto, Daniele; Parkkila, Taylor; Sebastianelli, Lorenzo; Guella, Graziano; Hendricks, Amber L; Cowan, James A; Sang, Lingzi; Mansy, Sheref S. - In: CHEMBIOCHEM. - ISSN 1439-7633. - STAMPA. - 23:14(2022). [10.1002/cbic.202200202]

Histidine Ligated Iron-Sulfur Peptides

Valer, Luca;Rossetto, Daniele;Guella, Graziano;Mansy, Sheref S
2022-01-01

Abstract

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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Valer, Luca; Rossetto, Daniele; Parkkila, Taylor; Sebastianelli, Lorenzo; Guella, Graziano; Hendricks, Amber L; Cowan, James A; Sang, Lingzi; Mansy, Sheref S
Histidine Ligated Iron-Sulfur Peptides / Valer, Luca; Rossetto, Daniele; Parkkila, Taylor; Sebastianelli, Lorenzo; Guella, Graziano; Hendricks, Amber L; Cowan, James A; Sang, Lingzi; Mansy, Sheref S. - In: CHEMBIOCHEM. - ISSN 1439-7633. - STAMPA. - 23:14(2022). [10.1002/cbic.202200202]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11572/351750
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