Premium
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.