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

血红素加氧酶（HO）利用分子氧和nadph -细胞色素P450还原酶（CPR）的还原等效物催化血红素降解。本研究的目的是表征NAPDH与CPR结合到血红素与HO结合的电子途径，确定HO-CPR复合物的结构。我们试图表征在HO反应中作为反应中间体的羟血红素到氧化还原血红素转化过程中NADPH到羟血红素的电子途径，并表征血红素各丙酸侧链在电子向血红素铁转移过程中的功能。遗憾的是，我们无法获得HO-CPR配合物的良好晶体，但我们找到了稳定这种瞬态配合物的条件。

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.