Dioxygen Binding to a Simple Myoglobin Model in Aqueous Solution | Zendy

Kano Koji | Zendy; Kitagishi Hiroaki | Zendy; Kodera Masahito | Zendy; Hirota Shun | Zendy

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Dioxygen Binding to a Simple Myoglobin Model in Aqueous Solution

Author(s) -

Kano Koji,

Kitagishi Hiroaki,

Kodera Masahito,

Hirota Shun

Publication year - 2005

Publication title -

angewandte chemie international edition

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.831

H-Index - 550

eISSN - 1521-3773

pISSN - 1433-7851

DOI - 10.1002/anie.200461609

Subject(s) - myoglobin , aqueous solution , chemistry , adduct , dimer , linker , transition metal dioxygen complex , pyridine , phosphate buffered saline , hemeprotein , polymer chemistry , stereochemistry , organic chemistry , heme , oxygen , chromatography , computer science , enzyme , operating system

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 O 2 adduct is 30.1 h in phosphate buffer at pH 7 and 25 °C.

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