Manganese hemoglobin: Allosteric effects in redox and ligation equilibria

C. Bull*, R. G. Fisher, Brian M Hoffman

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-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 languageEnglish (US)
Pages (from-to)140-145
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume59
Issue number1
DOIs
StatePublished - Jul 10 1974

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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