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 |
|---|---|
| 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 |
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ASJC Scopus subject areas
- Chemistry(all)
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Reverse Bohr effect on the oxygen-binding affinity of heme embedded in a bilayer of liposome as a hemoglobin model : PH-induced oxygen uptake and evolution by aqueous synthetic lipid-heme solution. / Yuasa, Makoto; Tani, Yuichiroh; Nishide, Hiroyuki; Tsuchida, Eishun.
In: Journal of the Chemical Society, Dalton Transactions, No. 8, 1987, p. 1917-1920.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Reverse Bohr effect on the oxygen-binding affinity of heme embedded in a bilayer of liposome as a hemoglobin model
T2 - PH-induced oxygen uptake and evolution by aqueous synthetic lipid-heme solution
AU - Yuasa, Makoto
AU - Tani, Yuichiroh
AU - Nishide, Hiroyuki
AU - Tsuchida, Eishun
PY - 1987
Y1 - 1987
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=37049090365&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=37049090365&partnerID=8YFLogxK
U2 - 10.1039/DT9870001917
DO - 10.1039/DT9870001917
M3 - Article
AN - SCOPUS:37049090365
SP - 1917
EP - 1920
JO - Dalton Transactions
JF - Dalton Transactions
SN - 1472-7773
IS - 8
ER -