Non-heme iron protein explained

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.

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,^[1] and aromatic amino acid hydroxylases.^[2]

• Major diiron enzymes include hemerythrin, some ribonucleotide reductases,^[3] some methane monooxygenases, purple acid phosphatases, and ferritin.^{[4] [5]}

See also

• Iron-binding proteins

References

1. 10.1021/cr960039f. Dioxygen Activation by Enzymes with Mononuclear Non-Heme Iron Active Sites. 1996. Que. Lawrence. Ho. Raymond Y. N.. Chemical Reviews. 96. 7. 2607–2624. 11848838.
2. 10.1021/cr040653o. Reaction Mechanisms of Mononuclear Non-Heme Iron Oxygenases. 2005. Abu-Omar. Mahdi M.. Loaiza. Aristobulo. Hontzeas. Nikos. Chemical Reviews. 105. 6. 2227–2252. 15941213.
3. 10.1021/cr020421u. Radical Initiation in the Class I Ribonucleotide Reductase: Long-Range Proton-Coupled Electron Transfer?. 2003. Stubbe. Joanne. Nocera. Daniel G.. Yee. Cyril S.. Chang. Michelle C. Y.. Chemical Reviews. 103. 6. 2167–2202. 12797828.
4. 10.1021/cr020622y. Synthetic Models for Non-Heme Carboxylate-Bridged Diiron Metalloproteins: Strategies and Tactics. 2004. Tshuva. Edit Y.. Lippard. Stephen J.. Chemical Reviews. 104. 2. 987–1012. 14871147.
5. 10.1021/cr9500489. Dioxygen Activation by Enzymes Containing Binuclear Non-Heme Iron Clusters. 1996. Wallar. Bradley J.. Lipscomb. John D.. Chemical Reviews. 96. 7. 2625–2658. 11848839.