Source of residual Bohr effect in hemoglobin oxidation

C. Bull, G. Goncher, C. S. Deutschman, B. M. Hoffman

Research output: Contribution to journalArticlepeer-review

Abstract

The hemoglobin oxidation Bohr effect is larger than the ligation Bohr effect, even when the former is corrected for any ionization of the water molecule bound to the ferric iron of methemoglobin. This residual oxidation Bohr effect is here shown to be solely caused by the influence of the positively charged ferriheme, and is abolished when the oxidized heme binds an anion. This result frees the formal equivalence of hemoglobin ligation and oxidation from the last apparent experimental discrepancy.

Original languageEnglish (US)
Pages (from-to)3128-3130
Number of pages3
JournalJournal of Biological Chemistry
Volume252
Issue number10
StatePublished - 1977

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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