8.A.252. The Heme Oxidase (HO) Family
HO1 catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron (Hwang et al. 2009). It affords protection against programmed cell death, and this cytoprotective effect relies on its ability to catabolize free heme and prevent it from sensitizing cells to undergo apoptosis (Gozzelino et al. 2010).
References associated with 8.A.252 family:
Gozzelino, R., V. Jeney, and M.P. Soares. (2010). Mechanisms of cell protection by heme oxygenase-1. Annu Rev Pharmacol Toxicol 50: 323-354. 20055707
Hwang, H.W., J.R. Lee, K.Y. Chou, C.S. Suen, M.J. Hwang, C. Chen, R.C. Shieh, and L.Y. Chau. (2009). Oligomerization is crucial for the stability and function of heme oxygenase-1 in the endoplasmic reticulum. J. Biol. Chem. 284: 22672-22679. 19556236
Niu, X., M. Wang, M. Wang, X. Liu, Y. Zhang, P. Zheng, S. Zhang, T. Liu, Z. Cao, and C. Zhang. (2025). Dracorhodin perochlorate sensitizes colorectal cancer to ferroptosis by activating HMOX1 and inhibiting the SLC7A11/GPX4 axis. Int Immunopharmacol 158: 114827. 40359890