Crystal structure analyses of cooperative oxygen-binding intermediates of giant hemoglobin

2014 Fiscal Year Final Research Report

• Project/Area Number: 25870200
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Structural biochemistry; Biophysics
• Research Institution: Tokyo Medical and Dental University
• Principal Investigator: NUMOTO Nobutaka 東京医科歯科大学, 難治疾患研究所, 助教 (20378582)
• Project Period (FY): 2013-04-01 – 2015-03-31
• 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

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.

Free Research Field

構造生物化学