Linearity of the hemoglobin oxidation Bohr effect

B. M. Hoffman, C. Bull

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

The hemoglobin oxidation Bohr effect below pH 7 is essentially proportional to the fraction of hemes oxidized, just as the ligation Bohr effect is proportional to fractional heme ligation. The reported nonlinear proton release during oxidation is shown to be an artifact resulting from the use of ferricyanide as oxidant. Published forms of the two state allosteric transition model for hemoglobin function have used several proton linkage schemes, and none are compatible with a linear proton release upon oxidation.

Original languageEnglish (US)
Pages (from-to)800-803
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Volume73
Issue number3
DOIs
StatePublished - 1976

ASJC Scopus subject areas

  • General

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