Dioxygen binding to a simple myoglobin model in aqueous solution

被引：85

作者：

Kano, K ^{[1
]}

Kitagishi, H

Kodera, M

Hirota, S

机构：

[1] Doshisha Univ, Dept Mol Sci & Technol, Kyoto 6100321, Japan

[2] Kyoto Pharmaceut Univ, Yamashima Ku, Kyoto 6078414, Japan

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2005年 / 44卷 / 03期

关键词：

cyclodextrins; inclusion compounds; metalloproteins; porphyrinoids; supramolecular chemistry;

D O I：

10.1002/anie.200461609

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Reversible binding of dioxygen occurs in aqueous solution to a myoglobin model composed of a porphinato iron(II) compound and a per-O-methylated β-cyclodextrin dimer with a pyridine linker (see picture). The dioxygen affinity of this system is 17.5 ± 1.7 Torr and the half-life of the O2 adduct is 30.1 h in phosphate buffer at pH 7 and 25°C. (Figure Presented).

引用

页码：435 / 438

页数：4

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