The proton iron-sulfur cluster environment of the [FeFe]-hydrogenase maturation protein HydF from Thermotoga neapolitana |
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Authors: | Marco Albertini Francesca Vallese Marilena Di Valentin Paola Berto Giorgio M Giacometti Paola Costantini Donatella Carbonera |
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Affiliation: | 1. Department of Chemical Sciences, University of Padova, Via Marzolo 1, 35131 Padova, Italy;2. Department of Biomedical Sciences, University of Padova, Viale G. Colombo 3, 35131 Padova, Italy;3. Department of Biology, University of Padova, Viale G. Colombo 3, 35131 Padova, Italy |
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Abstract: | FeFe]-hydrogenases contain a complex 4Fe–4S]-2Fe cluster (H-cluster) and are able to efficiently reduce protons to H2. Due to their potential exploitation for renewable energy production biotechnologies, significant efforts have been put into understanding the mechanisms driving the H-cluster assembly, which involves three conserved proteins. Among them, HydF works as scaffold upon which the H-cluster precursor is synthesized and carrier to deliver it to the hydrogenase, resulting in its activation. A FeS cluster binding sequence (CxHx46-53HCxxC) is conserved in all HydF proteins and should in principle provide four ligands to coordinate the Fe atom. However, we found that alternative metal coordination may exist in different HydF proteins and that only the three cysteines are strictly required, whereas the fourth ligand may vary and is, in any case, readily exchangeable. In this work we analyzed by EPR/HYSCORE the FeS cluster proton environment of HydF from Thermotoga neapolitana to determine the possible role of surrounding residues in the non-cysteinyl iron ligation of the protein. |
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Keywords: | Iron-sulfur proteins Hydrogenase HydF Iron-sulfur cluster coordination EPR |
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