PMID: 701084Jan 1, 1978Paper

Allosteric effect of o-iodobenzoate on hemoglobin

Hemoglobin
F TaketaM B Laver

Abstract

O-Iodobenzoate interacts non-covalently with hemoglobin and lowers the oxygen affinity of the protein. In contrast to 2,3-diphosphoglycerate or inositol hexaphosphate, its interaction does not depend upon the presence of free amino groups at the beta-chain amino terminals. Lysine beta82 is one of its oxygenation linked binding sites. As with the organic phosphates, the halogenated benzoate reacts preferentially with deoxy-hemoglobin to shift the allosteric equilibrium from R to T.

References

Jul 8, 1975·Biochemical and Biophysical Research Communications·R Baumann, E A Haller
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Aug 15, 1973·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·F Taketa
Jun 1, 1972·Archives of Biochemistry and Biophysics·A G Mauk, F Taketa
Sep 12, 1972·Biochemistry·R E BeneschN Maeda
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Sep 17, 1971·Biochemical and Biophysical Research Communications·P R CaldwellE R Jaffe
Feb 1, 1968·Proceedings of the National Academy of Sciences of the United States of America·R BeneschC I Yu
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Oct 1, 1958·Archives of Biochemistry and Biophysics·A ROSSI-FANELLI, E ANTONINI

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Citations

Apr 15, 1980·Journal of Molecular Biology·M F PerutzH S Rollema

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