Flexibility of the Coordination Geometry at the N-Site of Cu(Ⅱ)₂ Human Serum-Transferrin Induced by the Different Orientations of Arg124
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- Hata Toshiyuki
- Faculty of Pharmacy and Pharmaceutical Sciences, Fukuyama University
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- Shibata Yu
- Faculty of Life Science and Biotechnology, Fukuyama University
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- Okano Miku
- Faculty of Pharmacy and Pharmaceutical Sciences, Fukuyama University
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- Kodera Asako
- Faculty of Pharmacy and Pharmaceutical Sciences, Fukuyama University
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- Ueda Misato
- Faculty of Pharmacy and Pharmaceutical Sciences, Fukuyama University
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- Iwamoto Hiroshi
- Faculty of Life Science and Biotechnology, Fukuyama University
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- Tomida Hisao
- Faculty of Pharmacy and Pharmaceutical Sciences, Fukuyama University
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- Iwamoto Hiroyuki
- Faculty of Life Science and Biotechnology, Fukuyama University
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- Hirose Junzo
- Faculty of Pharmacy and Pharmaceutical Sciences, Fukuyama University
書誌事項
- タイトル別名
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- Flexibility of the Coordination Geometry at the N-Site of Cu(II)<sub>2</sub> Human Serum-Transferrin Induced by the Different Orientations of Arg124
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The ESR spectra of dicupric human serum-transferrin (serum-Tf) were measured from −20 to 37°C in the liquid state (56% glycerol at pH 7.6). Two coordination geometries (types B-1 and B-2) with different ESR parameters were present at the N-site. The contents of the coordination geometry of type B-1 at the N-site increased as the temperature increased. The equilibrium constant between the coordination geometries of types B-1 and B-2 was determined by ESR spectra. The enthalpy value from type B-2 to B-1 was +5.3 kcal/mol, as obtained from a van’t Hoff plot. The two conformational energies of the cluster models of the copper-binding site at the N-site of dicupric human serum-Tf, where the Arg124 residue was oriented in two different directions (conformations I and II), were calculated by Density Functional Theory, and the enthalpy value from conformation II to I was +2.1 kcal/mol. The enthalpy value was similar to that (+5.3 kcal/mol) obtained by the coordination geometrical change from type B-2 to B-1 in Cu(II)2 serum-Tf. In conformations I and II, the residue of Arg124 at the N-site is located either far from or near the copper-binding site, respectively, and in both cases the coordination geometry of the cupric ions at the N-site has changed from a flattened tetrahedron to a trigonal bipyramid. This result implies that the ESR spectral change from type B-2 to B-1 is caused by the presence of two different orientations of Arg124 in the change from conformation II to I.
収録刊行物
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- Biological & Pharmaceutical Bulletin
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Biological & Pharmaceutical Bulletin 38 (3), 358-364, 2015
公益社団法人 日本薬学会
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詳細情報 詳細情報について
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- CRID
- 1390282679611231488
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- NII論文ID
- 130004872273
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- NII書誌ID
- AA10885497
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- ISSN
- 13475215
- 09186158
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- NDL書誌ID
- 026193146
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- PubMed
- 25757916
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可