Structural and biochemical studies about electron pathways in heme oxygenase-redox counterpart complex

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Heme oxygenase (HO) catalyzes the heme degradation utilizing molecular oxygen and reducing equivalents from NADPH-cytochrome P450 reductase (CPR). The purposes of this study are the characterization of electron pathway between NAPDH bound to CPR to heme bound to HO, and the structure determination of HO-CPR complex. We attempted to characterize the electron pathway from NADPH to hydroxyheme in the conversion from hydroxyheme to verdoheme, which are reaction intermediates in HO reaction, and to characterize the function of each propionate side chain of heme in the electron transfer to the heme iron. Unfortunately, we could not obtain good crystals of HO-CPR complex, but we found the condition to stabilize this transient complex.