Dioxygen Binding to a Simple Myoglobin Model in Aqueous Solution

Abstract

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.