| Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2016: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2015: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2014: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Outline of Final Research Achievements |
We analyzed the functional properties of myoglobin and its mutant proteins reconstituted with heme cofactors possessing a heme Fe atom with a variety of electron densities. The study revealed that the oxygen (O2) affinities of the proteins are regulated by the electron density of the heme Fe atom (R(Fe)) in such a manner that the O2 affinity of the protein decreases, due to an increase in the O2 dissociation rate constant, with a decrease in the R(Fe). On the other hand, the carbon monoxide (CO) affinities of the proteins were almost independent of the R(Fe). As a result, the regulation of the O2/CO discrimination in the proteins is controlled by the R(Fe). Thus the electronic tuning of the intrinsic heme Fe reactivity through the R(Fe) plays a vital role in the regulation of the protein function, as the heme environment furnished by the nearby amino acid residues does. These findings pave the way to construct artificial blood substitute.
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