2001 Fiscal Year Final Research Report Summary
Relationship of function and higher order structure of abnormal hemoglobin.
| Project/Area Number |
10670115
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (C)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
General medical chemistry
|
|---|
| Research Institution | Kanazawa University |
|---|
Principal Investigator |
NAGAI Masako Kanazawa University, Faculty of Medicine, School of Health Sciences, Professor, 医学部, 教授 (60019578)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
SAKURAI Hiroshi Kanazawa University, Faculty of Medicine, School of Health Sciences, Associate Professor, 医学部, 助教授 (00225848)
|
|---|
| Project Period (FY) |
1998 – 2001
|
| Keywords | Hemoglobin / UVCD / UV resonance Raman / Allostery / Ouaternary structure transition / Aromatic amino acids / T-state marker / Oxygen equilibrium |
|---|
| Research Abstract |
In order to address the relationship between oxygen binding function (allostery) and quaternary structure changes of hemoglobin A (Hb A), we have studied on structure and function of abnormal hemoglobin by ultraviolet (UV) circular dichroism (CD) and UV resonance Raman (UVRR) spectroscopy. The results were summarized as follows :
(1) A study of quaternary structure change of Hb by UVCD : We examined UVCD spectra of abnormal hemoglobin with amino acid substitution at α1-β2 subunit interface (References, 1, 2).
(1) Heme and protein structure of Hb M Iwate and Hb M Boston characterized by UV and visible resonance Raman study (References, 3, 4).
(2) Structural and functional relationship of hemoglobin by UVRR : Tyr and Trp RR bands excited with 235nm changed upon deoxy->oxy(or CO) structure transition. We clarified which Tyr or Trp residue contributed to these changes using abnormal hemoglobin, NO and metal-hybrid Hb (References, 5-7).
From these results, we have elucidated that Tyr and/or Trp residues at α1-β2 subunit interface are critically important for hemoglobin allostery. These aromatic residues contribute not independently but cooperatively to higher order protein structure transition of hemoglobin.
|
