Iron-dependent redox enzyme

Iron-dependent redox enzyme refers to a broad and essential class of proteins that utilize iron ions, either within a heme group or as non-heme iron, to catalyze electron transfer and oxidation-reduction reactions. These enzymes are fundamental to life, participating in critical pathways such as the mitochondrial electron transport chain, DNA replication via ribonucleotide reductase, and the detoxification of drugs through the Cytochrome P450 system (Andreini et al., 2008; Guengerich, 2001). They also serve as key sensors and regulators, such as the prolyl hydroxylases that modulate the cellular response to hypoxia by regulating Hypoxia-Inducible Factor (HIF) (Kaelin & Ratcliffe, 2008). Dysregulation of iron-dependent enzymatic activity is implicated in various pathologies, including the promotion of tumor growth in cancer, the development of neurodegenerative diseases through oxidative damage, and inflammatory responses mediated by lipoxygenases (Dixon & Stockwell, 2014; Haeggström & Funk, 2011). Therapeutic strategies targeting these enzymes include the use of small-molecule inhibitors for treating anemia, asthma, and certain cancers, as well as iron chelators to manage iron overload (Maxwell & Eckardt, 2016). However, the structural similarity among different iron-binding sites and the widespread distribution of these enzymes present significant challenges for drug selectivity and safety (Hider & Kong, 2011).

Other names

Iron-containing oxidoreductaseHeme-dependent enzymeNon-heme iron enzymeIron-sulfur cluster proteinMetalloprotein redox enzyme

Inhibition of catalytic activity by binding to the active site, chelation of the essential iron cofactor, or competitive inhibition with substrates or co-substrates like alpha-ketoglutarate.