Structural and biochemical studies about electron pathways in heme oxygenase-redox counterpart complex
| Project/Area Number |
20770092
|
|---|
| Research Category |
Grant-in-Aid for Young Scientists (B)
|
| Allocation Type | Single-year Grants |
|---|
| Research Field |
Structural biochemistry
|
|---|
| Research Institution | Kurume University |
|---|
Principal Investigator |
SUGISHIMA Masakazu Kurume University, 医学部, 講師 (30379292)
|
|---|
| Project Period (FY) |
2008 – 2010
|
| Project Status |
Completed (Fiscal Year 2010)
|
| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2010: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2009: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2008: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
|
|---|
| Keywords | X線結晶解析 / 分子間相互作用 / 生体金属分子化学 / 電子伝達反応 / ヘムタンパク質 / 酵素反応中間体 |
|---|
| Research Abstract |
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.
|
Report
(4 results)
Research Products
(82 results)
