Molecular mechanism of transmembrane electron transfer catalyzed by a plant cytochrome b561
Project/Area Number |
22570142
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Functional biochemistry
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Research Institution | Kobe University |
Principal Investigator |
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Research Collaborator |
TAKEUCHI Fusako 神戸大学, 大学教育推進機構, 助教 (00448169)
|
Project Period (FY) |
2010 – 2012
|
Project Status |
Completed (Fiscal Year 2012)
|
Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2012: ¥650,000 (Direct Cost: ¥500,000、Indirect Cost: ¥150,000)
Fiscal Year 2011: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2010: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
|
Keywords | 金属タンパク質 / アスコルビン酸 / シトクロム b561 / ヘムタンパク質 / 電子伝達反応 / ビタミン C / シトクロムb561 / 膜タンパク質 / ビタミンC / 部位特異的変異体 / メタノール資化性酵母 / ビタミンC / モノデヒドロアスコルビン酸ラジカル / 電子伝達 |
Research Abstract |
We investigated Zea mayscytochrome b561 by employing the Pichia pastoris expression system to clarify the physiological roles of plant vacuole cytochromes b561 and the molecular mechanisms of their ascorbate-specific transmembrane electron transfer. We succeeded in expression and purification of Zea mayscytochrome b561. The detailed analyses of the electron transfer reactions with ascorbate and monodehydroascorbate radical by stopped-flow and pulse-radiolysis methods indicated that Zea mays cytochrome b561 has a similar molecular mechanism with that of animal neuroendocrine cytochrome b561 and that conserved amino acid residues have important roles for such ascorbate-specific transmembrane electron transfer reactions.
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Report
(4 results)
Research Products
(47 results)