Non-heme iron protein
In biochemistry, non-heme iron proteins describe families of enzymes that utilize iron at the active site but lack heme cofactors. Iron-sulfur proteins, including those that are enzymes, are not included in this definition. By tradition, non-heme iron enzymes refers to those involved in oxygen activation,[1] such as those described below.
Some non-heme iron proteins contain one Fe at their active sites, others have pairs of Fe centers:
- Many mono-Fe proteins are alpha-ketoglutarate-dependent hydroxylases. Major examples are the lipoxygenases, isopenicillin N synthase, protocatechuate 3,4-dioxygenase, deacetoxycephalosporin-C synthase,[2] and aromatic amino acid hydroxylases.[3][4]
- Diiron enzymes include hemerythrin, some ribonucleotide reductases,[5] and some methane monooxygenases,[6] Some of these active sites are mixed valence (Fe(II)Fe(III)) and some are diferrous (Fe(II)Fe(II)).[7]
Oxygenation of hemerythrin, a non-heme diiron protein.
Other non-heme iron proteins
References
- ↑ McLachlan, Jill; Hammer, Stephan C. (2025). "Non-heme iron enzymes step into the spotlight". Nature Chemical Biology. 21 (11): 1650–1651. doi:10.1038/s41589-025-02004-0. PMID 40846993.
- ↑ Que, Lawrence; Ho, Raymond Y. N. (1996). "Dioxygen Activation by Enzymes with Mononuclear Non-Heme Iron Active Sites". Chemical Reviews. 96 (7): 2607–2624. Bibcode:1996ChRv...96.2607Q. doi:10.1021/cr960039f. PMID 11848838.
- ↑ Abu-Omar, Mahdi M.; Loaiza, Aristobulo; Hontzeas, Nikos (2005). "Reaction Mechanisms of Mononuclear Non-Heme Iron Oxygenases". Chemical Reviews. 105 (6): 2227–2252. doi:10.1021/cr040653o. PMID 15941213.
- ↑ Tshuva, Edit Y.; Lippard, Stephen J. (2004). "Synthetic Models for Non-Heme Carboxylate-Bridged Diiron Metalloproteins: Strategies and Tactics". Chemical Reviews. 104 (2): 987–1012. Bibcode:2004ChRv..104..987T. doi:10.1021/cr020622y. PMID 14871147.
- ↑ Stubbe, Joanne; Nocera, Daniel G.; Yee, Cyril S.; Chang, Michelle C. Y. (2003). "Radical Initiation in the Class I Ribonucleotide Reductase: Long-Range Proton-Coupled Electron Transfer?". Chemical Reviews. 103 (6): 2167–2202. Bibcode:2003ChRv..103.2167S. doi:10.1021/cr020421u. PMID 12797828.
- ↑ Wallar, Bradley J.; Lipscomb, John D. (1996). "Dioxygen Activation by Enzymes Containing Binuclear Non-Heme Iron Clusters". Chemical Reviews. 96 (7): 2625–2658. Bibcode:1996ChRv...96.2625W. doi:10.1021/cr9500489. PMID 11848839.
- ↑ Skirboll, Sydney S.; Ledinina, Anastasia E.; Makris, Thomas M. (2026). "Heme oxygenase-like dimetal oxidases and oxygenases". Biochemical Society Transactions. 54 (3): 231–243. doi:10.1042/BST20253134. PMC 13108848. PMID 41823132.
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