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High-resolution crystal structures of the heme-binding domain of cytochrome b5 from porcine liver
https://repo.qst.go.jp/records/72113
https://repo.qst.go.jp/records/7211372b5f33a-05af-40d7-95fe-0a138c8d1571
| Item type | 会議発表用資料 / Presentation(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2017-01-05 | |||||
| タイトル | ||||||
| タイトル | High-resolution crystal structures of the heme-binding domain of cytochrome b5 from porcine liver | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_c94f | |||||
| 資源タイプ | conference object | |||||
| アクセス権 | ||||||
| アクセス権 | metadata only access | |||||
| アクセス権URI | http://purl.org/coar/access_right/c_14cb | |||||
| 著者 |
平野, 優
× 平野, 優× 木村, 成伸(茨城大学)× 玉田, 太郎× 平野 優× 玉田 太郎 |
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| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | Mammalian microsomal cytochrome b5 (b5) has multiple electron transfer partners that function in various electron-transfer reactions, such as lipid unsaturation, cholesterol synthesis and drug metabolism. Four crystal structures of the solubilized heme-binding domain of b5 from porcine liver were determined at sub-angstrom resolution (0.76-0.95 Å) in two crystal forms for both the oxidized and reduceed states. The high-resolution structures clearly displayed the electron density of H atoms in some amino acid residues and the heme molecule. Unrestrained refinement of the bond lengths revealed that the protonation states of the heme propionate group may be involved in stabilization of the heme redox properties. The heme Fe coordination geometry did not show significant differences between the oxidized and reduced structures. However, structural differences between oxidized and reduced states were observed in the hydrogen-bond network around the axial ligand His68. | |||||
| 会議概要（会議名, 開催地, 会期, 主催者等） | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | 第5回回折構造生物国際シンポジウム | |||||
| 発表年月日 | ||||||
| 日付 | 2016-08-08 | |||||
| 日付タイプ | Issued | |||||
