| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2012: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2011: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2010: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Research Abstract |
The CuA site in cytochrome C oxidase (COX) contains a binuclear copper center, which is composed of two bridging Cys residues forming a Cu_2S_2 diamond cluster. We designed this copper configuration in the de novo designed 4-helix bundled protein. The designed protein exhibited the same UV vis and ESR spectra as those of COX, indicating that we successfully constructed the Cu_2S_2 diamond cluster in the 4-helix bundled protein. Next, we designed a metal configuration from Zn-Cu superoxide dismutase or hemocyanin. We placed six His residues in the designed protein. The designed protein bound one Cu ion. Then, we added Cys residue to monitor the metal binding. We obtained an evidence that shows this mutant protein might bind two Cu ions or Cu and Zn ions simultaneously. The Cys residue might determine the position of Cu ion in the protein. A new strategy to design the plural metal bindings can be proposed using one Cys residue. The detail analyses are required, we are able to construct the metal binding following the new design method.
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