Affiliation:
1. Institut Pasteur, Université Paris Cité, CNRS UMR6047, Stress Adaptation and Metabolism Unit, Department of Microbiology , F-75015 Paris, France
Abstract
Abstract
Iron–sulfur (Fe–S) clusters are inorganic ubiquitous and ancient cofactors. Fe–S-bound proteins contribute to most cellular processes, including DNA replication and integrity, genetic expression and regulation, metabolism, biosynthesis, and most bioenergetics systems. Also, Fe–S proteins hold a great biotechnological potential in metabolite and chemical production, including antibiotics. From classic biophysics and spectroscopy methodologies to recent development in bioinformatics, including structural modeling and chemoproteomics, our capacity to predict and identify Fe–S proteins has spectacularly increased over the recent years. Here, these developments are presented and collectively used to update the composition of Escherichia coli Fe–S proteome, for which we predict 181 occurrences, i.e. 40 more candidates than in our last catalog, and equivalent to 4% of its total proteome. Besides, Fe–S clusters can be targeted by redox active compounds or reactive oxygen and nitrosative species, and even be destabilized by contaminant metals. Accordingly, we discuss how cells handle damaged Fe–S proteins, i.e. degradation, recycling, or repair.
Funder
Centre National de la Recherche Scientifique
Publisher
Oxford University Press (OUP)
Subject
Metals and Alloys,Biochemistry,Biomaterials,Biophysics,Chemistry (miscellaneous)
Reference58 articles.
1. Iron-Sulfur Proteins: Ancient Structures, Still Full of Surprises;Beinert;JBIC,2000
2. Structural Evidence for a [4Fe-5S] Intermediate in the Non-Redox Desulfuration of Thiouracil;Zhou;Angew. Chem. Int. Ed.,2021
3. An Unexpected P-Cluster Like Intermediate En Route to the Nitrogenase FeMo-Co;Jenner;Chem. Sci.,2021
4. Double-Cubane [8Fe9S] Clusters: A Novel Nitrogenase-Related Cofactor in Biology;Jeoung;ChemBioChem,2020
5. ATP-Dependent Substrate Reduction at an [Fe8S9] Double-Cubane Cluster;Jeoung,2018
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