| Project/Area Number |
15380083
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (B)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
Bioproduction chemistry/Bioorganic chemistry
|
|---|
| Research Institution | KYOTO UNIVERSITY |
|---|
Principal Investigator |
MIYOSHI Hideto Kyoto University, Agriculture, Associate Professor, 農学研究科, 助教授 (20190829)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
KITA Kiyoshi University of Tokyo, Medicine, Professor, 大学院・医学系研究科, 教授 (90134444)
|
|---|
| Project Period (FY) |
2003 – 2004
|
| Project Status |
Completed (Fiscal Year 2004)
|
| Budget Amount *help |
¥13,700,000 (Direct Cost: ¥13,700,000)
Fiscal Year 2004: ¥5,300,000 (Direct Cost: ¥5,300,000)
Fiscal Year 2003: ¥8,400,000 (Direct Cost: ¥8,400,000)
|
|---|
| Keywords | Respiratory Inhibitor / Respiratory Enzymes / Mitochondria / アセトゲニン / 構造活性相関 |
|---|
| Research Abstract |
To identify the binding subunit of fenpyroximate, a very potent inhibitor of bovine heart mitochondrial complex I, we synthesized ^3H-labeled photolabile fenpyroximate ([^3H](trifluoromethyl)-phenyldiazirinyl fenpyroximate, TDF). TDF appeared to elicit very potent inhibition of bovine heart mitochondrial complex I being nearly equivalent to that of fenpyroximate.
On the basis of photoaffinity studies with bovine heart complex I in collaboration with Dr.Takao Yagi (The Scripps Research Institute, USA), the binding site of TDF was shown to be subunit ND5 which is thought to exist in membrane arm of the enzyme. Since antibody to the C-terminal region of the ND5 subunit only weakly recognized the subunit, we identified the ND5 by 2D-electrophoresis (SDS-PAGE). Our result is the first study wherein the subunit located in membrane arm was identified as the inhibitor binding subunit. Our study strongly suggests that subunit(s) located in membrane arm may be involved in the proton-pumping activity of complex I.
|
