Cytochrome oxidase and proton translocation
| Project/Area Number |
02454559
|
|---|
| Research Category |
Grant-in-Aid for General Scientific Research (B)
|
| Allocation Type | Single-year Grants |
|---|
| Research Field |
生物物性学
|
|---|
| Research Institution | KYOTO UNIVERSITY |
|---|
Principal Investigator |
ORII Yutaka Kyoto University, Fac. of Medicine, Associate Professor., 医学部, 助教授 (60028149)
|
|---|
| Project Period (FY) |
1990 – 1991
|
| Project Status |
Completed (Fiscal Year 1991)
|
| Budget Amount *help |
¥6,900,000 (Direct Cost: ¥6,900,000)
Fiscal Year 1991: ¥1,700,000 (Direct Cost: ¥1,700,000)
Fiscal Year 1990: ¥5,200,000 (Direct Cost: ¥5,200,000)
|
|---|
| Keywords | cytochrome oxidase / flow-flash / proton pump / anaerobiosis / oxygen / hydrogen peroxide / フロ-フラッシュ法 / プロトポンプ / 嫌気條件 / プロトン / フラッシュフオトリシス / 生体エネルギ- / 化学浸透説 |
|---|
| Research Abstract |
1. In order to collect fundamental data for establishing the system to measure the concentration of tissue oxygen by utilizing a laser flash photolysis technique, a rapid-scan spectrophotometer, double-flash spectrophotometer and a time-resolved absorption spectrophotometer were constructed. Both rapid-scan and double-flash apparatuses are of the highest performance ever built in the world; the former allows to record 512 consecutive absorption and reflectance spectra of a 200-nm span at the maximum time resolution of 1 ms, and the latter has a time resolution of 1mus. These apparatuses have been used extensively in wide areas of related fields. One of remarkable achievements is the finding of the functional role of yeast flavohemoglobin as an oxygen sensor.
2. Oxygenation process of myoglobin contained in meat was followed spectrally by using the rapid-scan apparatus in combination with an optical probe made of optical fibers. Upon exposure of the interior to air oxygen by dissecting a meat lump, a color of the cut surface changes from dark brown to bright red. The spectral changes clearly indicate the formation of oxymyoglobin which is characterized by a growth of peaks at 582 and 540 nm with an isosbestic point at 591 nm. The absorbance changes followed at 582 nm against 591 nm as reference are invariably biphasic.
3. The photodissociation of oxyhemoglobin and its recombination process have been studied by utilizing all of the apparatuses constructed and relevant kinetic data were collected at varying oxygen concentrations. These kinetic parameters are correlated with the oxygen concentration and the procedure to measure the oxygen concentration in solution has been established. Based on these data a variety of problems involved in the determination of tissue oxygen concentrations are revealed.
|
Report
(3 results)
Research Products
(24 results)
