Premium
The BOHR effect before Perutz
Author(s) -
Brunori Maurizio
Publication year - 2012
Publication title -
biochemistry and molecular biology education
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.34
H-Index - 39
eISSN - 1539-3429
pISSN - 1470-8175
DOI - 10.1002/bmb.20629
Subject(s) - bohr effect , hemoglobin , chemistry , bohr model , crystallography , molecule , oxygen–haemoglobin dissociation curve , biochemistry , organic chemistry , physics , quantum mechanics
Before the outbreak of World War II, Jeffries Wyman postulated that the Bohr effect in hemoglobin demanded the oxygen linked dissociation of the imidazole of two histidines of the polypeptide. This proposal emerged from a rigorous analysis of the acid–base titration curves of oxy‐ and deoxy‐hemoglobin, at a time when the information on the chemistry and structure of the protein was essentially nil. The magnetochemical properties of hemoglobin led Linus Pauling to hypothesize that the (so called) Bohr histidines were coordinated to the heme iron in the fifth and sixth positions; and Wyman shared this opinion. However, this structural hypothesis was abandoned in 1951 when J. Wyman and D. W. Allen proposed the p K shift of the oxygen linked histidines to be the result of “… a change of configuration of the hemoglobin molecule as a whole accompanying oxygenation.” This shift in paradigm, that was published well before the 3D structure of hemoglobin was solved by M.F. Perutz, paved the way to the concept of allostery. After 1960 the availability of the crystallographic structure opened new horizons to the interpretation of the allosteric properties of hemoglobin.