Manganese hemoglobin: Allosteric effects in redox and ligation equilibria

C. Bull; R. G. Fisher; B. M. Hoffman

doi:10.1016/S0006-291X(74)80185-3

Manganese hemoglobin: Allosteric effects in redox and ligation equilibria

C. Bull^*, R. G. Fisher, B. M. Hoffman

^*Corresponding author for this work

Chemistry

Research output: Contribution to journal › Article › peer-review

33 Scopus citations

Abstract

Allosteric effects have been observed in the binding of ligands to manganese substituted hemoglobin. Redox measurements indicate a preferred binding of organic phosphates to reduced manganese hemoglobin and the existence of a Bohr effect. The redox n-values, with and without organic phosphate, are similar to those of hemoglobin at all pH values. Differential pH titration of manganese hemoglobin and its nitric oxide derivative demonstrates the existence of both alkaline and acid Bohr effects in the binding of ligands.

Original language	English (US)
Pages (from-to)	140-145
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	59
Issue number	1
DOIs	https://doi.org/10.1016/S0006-291X(74)80185-3
State	Published - Jul 10 1974

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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abstract = "Allosteric effects have been observed in the binding of ligands to manganese substituted hemoglobin. Redox measurements indicate a preferred binding of organic phosphates to reduced manganese hemoglobin and the existence of a Bohr effect. The redox n-values, with and without organic phosphate, are similar to those of hemoglobin at all pH values. Differential pH titration of manganese hemoglobin and its nitric oxide derivative demonstrates the existence of both alkaline and acid Bohr effects in the binding of ligands.",

author = "C. Bull and Fisher, {R. G.} and Hoffman, {B. M.}",

note = "Funding Information: MnIIIHb and to Professor Paul Loach for helpful discussions. C. B. is a predoctoral trainee of the USPHS~ administered by the National Institutes of Health, training grant GM00626. This work was supported by the National Institutes of Health, Grant HL-13531.",

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AU - Hoffman, B. M.

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PY - 1974/7/10

Y1 - 1974/7/10

N2 - Allosteric effects have been observed in the binding of ligands to manganese substituted hemoglobin. Redox measurements indicate a preferred binding of organic phosphates to reduced manganese hemoglobin and the existence of a Bohr effect. The redox n-values, with and without organic phosphate, are similar to those of hemoglobin at all pH values. Differential pH titration of manganese hemoglobin and its nitric oxide derivative demonstrates the existence of both alkaline and acid Bohr effects in the binding of ligands.

AB - Allosteric effects have been observed in the binding of ligands to manganese substituted hemoglobin. Redox measurements indicate a preferred binding of organic phosphates to reduced manganese hemoglobin and the existence of a Bohr effect. The redox n-values, with and without organic phosphate, are similar to those of hemoglobin at all pH values. Differential pH titration of manganese hemoglobin and its nitric oxide derivative demonstrates the existence of both alkaline and acid Bohr effects in the binding of ligands.

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Manganese hemoglobin: Allosteric effects in redox and ligation equilibria

Abstract

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