Iron-sulfur cluster protein (Fe-S protein)

Iron-sulfur (Fe-S) cluster proteins are a fundamental class of proteins characterized by the presence of iron-sulfur centers, which serve as versatile prosthetic groups (Lill, R., 2009, Nature). These proteins are essential for life, participating in critical biological processes such as electron transfer in the mitochondrial respiratory chain, enzymatic catalysis, and the sensing of ambient oxygen and iron levels (Beinert, H., et al., 1997, Science). In humans, they are involved in diverse pathways including the citric acid cycle, DNA replication, and repair (Rouault, T. A., 2015, Nature Reviews Molecular Cell Biology). Dysregulation or genetic defects in Fe-S cluster biogenesis lead to various pathologies, most notably Friedreich's ataxia and certain types of anemia and cancer (Braymer, J. J., & Lill, R., 2017, Chemical Reviews). From a pharmacological perspective, Fe-S proteins like those in Complex I are targeted by widely used drugs such as metformin to manage metabolic disorders (El-Mir, M. Y., et al., 2000, Journal of Biological Chemistry). Their central role in cellular energetics makes them significant targets for developing therapies against cancer and metabolic diseases, though their ubiquity poses challenges for achieving tissue-specific targeting.

Other names

Iron-sulfur proteinsFe-S proteinsNon-heme iron proteinsFerredoxins

Inhibition of mitochondrial electron transport chain complexes, disruption of iron-sulfur cluster assembly, or modulation of redox-active sites.