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Updated: Apr 19, 2026

EPR Monitored Redox Titration of the Cofactors of Saccharomyces cerevisiae Nar1
Published on: November 26, 2014
[Iron and sulfur in proteins. How does the cell build Fe-S clusters, cofactors essential for life?]
Béatrice Py1, Frédéric Barras1
1Laboratoire de Chimie Bactérienne, UMR 7283 CNRS-Aix-Marseille Université, Institut de Microbiologie de la Méditerranée, 31, chemin Joseph Aiguier, 13009 Marseille, France.
Abstract:
Iron-sulfur clusters (Fe-S) are ubiquitous cofactors present in numerous proteins of most living organisms. By way of an example, the E. coli bacterium synthesizes more that 130 different types of Fe-S proteins. Fe-S proteins are involved in a great diversity of biological processes, ranging from respiration, photosynthesis, central metabolism, to genetic expression and genomic stability. Proteins can acquire spontaneously Fe-S clusters in vitro, but in vivo, dedicated molecular machineries are necessary. Dysfunction of these machineries alters cellular capacities leading to lethality in bacteria and severe pathologies in humans. In this review we will describe how cells make Fe-S clusters and deliver them to clients proteins. The importance of Fe-S clusters homeostasis will be illustrated by reporting a list of cellular dysfunctions associated with mutations altering either Fe-S proteins or Fe-S biogenesis machineries.
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