2004 Fiscal Year Final Research Report Summary
Extreme Functionalization of Hemoproteins upon the Direct Chemical Modification to Heme Framework
| Project/Area Number |
14380291
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (B)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
Bioorganic chemistry
|
|---|
| Research Institution | Kyushu University |
|---|
Principal Investigator |
HAYASHI Takashi Kyushu University, Faculty of Engineering, Associate Professor, 大学院・工学研究院, 助教授 (20222226)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
HISAEDA Yoshio Kyushu University, Faculty of Engineering, Professor, 大学院・工学研究院, 教授 (70150498)
|
|---|
| Project Period (FY) |
2002 – 2004
|
| Keywords | myoglobin / reconstitution / artificial heme / iron porphyicene / dioxygen affinit / peroxidase / carbon monoxide affinity / prosthetic group |
|---|
| Research Abstract |
The incorporation of an artificially created heme into an apohemoprotein is a unique method for introducing a new chemical function into a protein. In this project, we mainly focused on a modification of heme framework to improve the function and/or create a new function in myoglobin. The summary of our recent results are shown as follows:
1.An iron porphycene as a structural isomer of the heme was inserted into apomyoglobin. The obtained reconstituted myoglobin showed an extremely high dioxygen affinity.
2.The reconstituted myoglobin with the iron porphycene showed peroxidase/peroxygenase activity. In addition, the compound III formation in the presence of hydrogen peroxide was firstly observed in myoglobin. Furthermore, a hybrid myoglobin which was prepared by heme-propionate modification and amino-acid mutation showed high peroxidase activity and is a good catalyst toward bisphenol A degradation.
3.Unusual dioxygen selectivity was obtained by introducing a hydrophobic cluster at the terminal two heme-propionate side chains.
These results suggest that the replacement of native heme with an artificially created prosthetic group will serve as a new way to create a functionalized hemoprotein.
|
