Heterogeneity between Two α Subunits of α2β2 Human Hemoglobin and O2 Binding Properties: Raman, 1H Nuclear Magnetic Resonance, and Terahertz Spectra

• Material Type: 文書・図像類
• Title: Heterogeneity between Two α Subunits of α2β2 Human Hemoglobin and O2 Binding Properties: Raman, 1H Nuclear Magnetic Resonance, and Terahertz Spectra
• Author/Editor: Nagatomo, Shigenori; Saito, Kazuya; Yamamoto, Kohji; Ogura, Takashi; Kitagawa, Teizo; Nagai, Masako
• Author Heading: Nagatomo, Shigenori; Saito, Kazuya; Yamamoto, Kohji; Ogura, Takashi; Kitagawa, Teizo; Nagai, Masako
• Publication, Distribution, etc.: American Chemical Society
• Publication Date: 2017-10-24
• Publication Date (W3CDTF): 2017-10-24
• Alternative Title: Heterogeneity between Two α Subunits of α2β2 Human Hemoglobin and O2 Binding Properties: Raman, 1H Nuclear Magnetic Resonance, and Terahertz Spectra
• Periodical title: Biochemistry
• No. or year of volume/issue: 56 46
• Volume: 56
• Issue: 46
• Pages: 6125-6136
• ISSN (Periodical Title): ISSN : 0006-2960
• Text Language Code: eng
• Target Audience: 一般
• Note (General): Following a previous detailed investigation of the β subunit of α2β2 human adult hemoglobin (Hb A), this study focuses on the α subunit by using three natural valency hybrid α(Fe2+-deoxy/O2)β(Fe3+) hemoglobin M (Hb M) in which O2 cannot bind to the β subunit: Hb M Hyde Park (β92His → Tyr), Hb M Saskatoon (β63His → Tyr), and Hb M Milwaukee (β67Val → Glu). In contrast with the β subunit that exhibited a clear correlation between O2 affinity and Fe2+− His stretching frequencies, the Fe2+−His stretching mode of the α subunit gave two Raman bands only in the T quaternary structure. This means the presence of two tertiary structures in α subunits of the α2β2 tetramer with T structure, and the two structures seemed to be nondynamical as judged from terahertz absorption spectra in the 5−30 cm−1 region of Hb M Milwaukee, α(Fe2+-deoxy)β(Fe3+). This kind of heterogeneity of α subunits was noticed in the reported spectra of a metal hybrid Hb A like α(Fe2+-deoxy)β(Co2+) and, therefore, seems to be universal among α subunits of Hb A. Unexpectedly, the two Fe−His frequencies were hardly changed with a large alteration of O2 affinity by pH change, suggesting no correlation of frequency with O2 affinity for the α subunit. Instead, a new Fe2+−His band corresponding to the R quaternary structure appeared at a higher frequency and was intensified as the O2 affinity increased. The high-frequency counterpart was also observed for a partially O2-bound form, α(Fe2+- deoxy)α(Fe2+-O2)β(Fe3+)β(Fe3+), of the present Hb M, consistent with our previous finding that binding of O2 to one α subunit of T structure α2β2 tetramer changes the other α subunit to the R structure.
• Access Restrictions: 限定公開
• Rights (production): copyright 2017 American Chemical Society
• Related Material (DOI): 10.1021/acs.biochem.7b00733
• Data Provider (Database): 国立情報学研究所 : 学術機関リポジトリデータベース（IRDB）（機関リポジトリ）; https://irdb.nii.ac.jp
• Original Data Provider (Database): 福井大学 : 福井大学学術機関リポジトリ