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ERIC Number: EJ991476
Record Type: Journal
Publication Date: 2012
Pages: 3
Abstractor: As Provided
Reference Count: 23
ISSN: ISSN-1470-8175
The BOHR Effect before Perutz
Brunori, Maurizio
Biochemistry and Molecular Biology Education, v40 n5 p297-299 Sep-Oct 2012
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 pK 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. (Contains 1 figure.)
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Publication Type: Journal Articles; Reports - Evaluative
Education Level: N/A
Audience: N/A
Language: English
Sponsor: N/A
Authoring Institution: N/A