The molecular mechanism of electron flow to mitochondria electron transfer fravoprotein
| Project/Area Number |
61570049
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
General physiology
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| Research Institution | Kumamoto university |
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Principal Investigator |
NISHINA Yasuzo Kumamoto University Medical School, 医学部, 助教授 (50112553)
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| Co-Investigator(Kenkyū-buntansha) |
SHIGA Kiyoshi Kumamoto University Medical School, 医学部, 教授 (40028527)
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| Project Period (FY) |
1986 – 1988
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| Project Status |
Completed (Fiscal Year 1988)
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| Budget Amount *help |
¥2,400,000 (Direct Cost: ¥2,400,000)
Fiscal Year 1988: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 1987: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1986: ¥1,100,000 (Direct Cost: ¥1,100,000)
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| Keywords | Flavoprotein / FAD / ラマンスペクトル / electron transfer flavoprotein / general acyl CoA dehydrogenase |
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| Research Abstract |
(1) A simple method for preparation of the apoprotein of hog kindney mitochondria electron transfer flavoprotein was established.
(2) The equilibrium and kinetic studies on the complexation between the apoprotein and GAD were carried out by measuring the fluorescence of FAD. The apparent binding rate constant (K_<obs>) with FAD was measured, immediately after the dilution of the apoETF. The value of K_<obs> increased linearly upon the in-crease of the concentration of apoETF. The time dependency of the value of K_<obs> after dilution of the apoETF, was obtained. The value of K_<obs> decreased with the passage of time. These phenomena suggest that the following equilibrium exist.
+ <double arrow>
+ FDA <double arrow>holoETF
(3) General acyl-Coa dehydrogenase (GAD) is one of the dehydrogenases which donate electrons to ETF. GAD, in any three redox states, forms charge transfer complexes with products. These charge transfer complexes are important species in the catalytic reaction mechanism. So, in order to clarify the structure of the complex, we observed the resonance Raman spectra of the complex of oxidized gad with acetoacetyl-coa. several raman bands of fad were resonance-enhanced by the charge transfer band. The intensity enhancement was remarkable for the Raman bands at 1583 and 1550 cm^<-1>, which are known to involve the vibrational dis-placements of the N(5) and C(4a) atoms of isoalloxazine. These features of resonance enhancement of Raman intensity suggest acetoacetyl-Coa lies along the N(5)-C(4a).
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Report
(4 results)
Research Products
(15 results)
