Abstract
The oxygen-binding affinity (p1/2; oxygen pressure at 50% binding for the heme) of a heme derivative embedded in a bilayer of natural phospholipid liposomes was influenced by the solution pH: the p1/2 value of the liposome-lipid-heme increased with pH {Bohr coefficient, r = d[log(p1/2)]d(pH) = +0.09 to +0.32}, which is the reverse of the Bohr effect for hemoglobin. This pH dependence was affected by the composition of the liposome-lipid-heme. Its mechanism is discussed in relation to the surrounding lipid bilayer structure and protonation equilibrium of the imidazole ligand. pH-induced oxygen-uptake and -evolution was observed, in a process which was sensitive to ±1 unit of pH change at pH 7.
Original language | English |
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Pages (from-to) | 1917-1920 |
Number of pages | 4 |
Journal | Journal of the Chemical Society, Dalton Transactions |
Issue number | 8 |
DOIs | |
Publication status | Published - 1987 |
ASJC Scopus subject areas
- Chemistry(all)