Crystal structure analyses of cooperative oxygen-binding intermediates of giant hemoglobin
| Project/Area Number |
25870200
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Structural biochemistry
Biophysics
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| Research Institution | Tokyo Medical and Dental University |
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Principal Investigator |
NUMOTO Nobutaka 東京医科歯科大学, 難治疾患研究所, 助教 (20378582)
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| Project Period (FY) |
2013-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2014: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
Fiscal Year 2013: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | ヘモグロビン / 協同性 / 構造変化 / X線結晶構造解析 / 中間体 / 構造生物 / 四次構造 |
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| Outline of Final Research Achievements |
The crystals of the giant hemoglobin (V2Hb) from an invertebrate were transformed from the oxygenated to the deoxygenated state in keeping a crystalline structure. We have performed X-ray crystal structure analyses of various intermediate states between the oxy and deoxy forms of V2Hb. The electron densities of the oxygen molecules at the heme pockets (oxygen binding sites) gradually became very week or disappeared. The ternary structural changes occur primarily at AB-loop region of some subunits. The quaternary rearrangement of V2Hb might arise just before a complete dissociation of all the oxygen molecules from all the subunits.
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Report
(3 results)
Research Products
(7 results)
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[Journal Article] The structure of a deoxygenated 400 kDa hemoglobin reveals ternary and quaternary structural changes of giant hemoglobins2014
Author(s)
Numoto, N., Nakagawa, T., Ohara, R., Hasegawa, T., Kita, A., Yoshida, T., Maruyama, T., Imai, K., Fukumori, Y., and Miki, K.
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Journal Title
Acta Crystallogr D Biol Crystallogr.
Volume: 70
Issue: 7
Pages: 1823-1831
DOI
Related Report
Peer Reviewed
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