Iron-sulfur cluster enzyme (Fe-S enzyme) (Fe-S enzyme)

Iron-sulfur cluster enzymes are a diverse and essential class of proteins characterized by the presence of iron-sulfur (Fe-S) centers, which serve as critical prosthetic groups for electron transfer, catalysis, and environmental sensing [Beinert et al., 1997, Science]. These enzymes are integral to primary metabolic pathways, most notably within the mitochondrial respiratory chain (Complexes I, II, and III) and the citric acid cycle (Aconitase), where they facilitate the movement of electrons and the conversion of substrates [Lill, 2009, Nature]. Beyond metabolism, Fe-S clusters are critical for DNA maintenance, as they are found in various polymerases and helicases required for replication and repair [Rouault, 2015, Nature Chemical Biology]. In clinical contexts, defects in the assembly or function of these enzymes lead to severe conditions such as Friedreich's ataxia, sideroblastic anemia, and various mitochondrial encephalopathies [NIH, 2023]. Pharmacologically, these enzymes are targeted by drugs like metformin, which inhibits Complex I, and are also sensitive to oxidative stress and heavy metal interference, making them significant focal points for both therapeutic intervention and toxicological study [PubChem, 2024]. Their fundamental role in cellular energy and genetic integrity makes them high-priority targets in oncology and metabolic disease research [PubMed, 2022].

Other names

Iron-sulfur protein [UniProt]Fe-S protein [PubMed]Non-heme iron-sulfur protein [Wikipedia]Iron-sulfur cluster-containing protein [PubMed]

Inhibition of mitochondrial respiratory chain complexes, modulation of iron-sulfur cluster biogenesis, or direct binding to the iron-sulfur center to disrupt enzymatic activity [PubChem, 2024].