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. 2011 Mar 15;14(6):1039–1047. doi: 10.1089/ars.2010.3436

FIG. 3.

FIG. 3.

Regulation of heme binding by the HRMs in HO2. Conversion from the thiol(ate) to the disulfide state appears to involve a sulfenate intermediate (33). The oxidized disulfide state has much higher affinity for heme than the reduced state. The midpoint redox potential for the SS/2RSH couple is −200 mV (22). (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article at www.liebertonline.com/ars).