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• W2617362693 abstract "This chapter discusses the relationship between molecular structure and physiological activity of hemoglobins. The reactions of hemoglobins have been interpreted in terms of the imidazole, steric hindrance, heme–heme interaction and intermediate compound hypotheses, which have had wide acceptance. The reduction of hematin to heme markedly decreases the acid strength of one or both of the propionate side chains. Nickel mesoporphyrin, which can only combine through its propionate side chains, links with a group or groups in horse apohemoglobin with imidazolium characteristics. The group in apomyoglobin binding the heme iron is more likely to be of the nature of a β or ϒ carboxyl than an imidazole group. The chapter presents an interpretation of the sigmoid shape of the oxygen dissociation curve, the Bohr Effect, the alkaline stability, and the change of molecular shape on oxygenation, in terms of labile electrostatic linkages between the heme propionate groups and imidazolium side chains of horse apohemoglobin." @default.
• W2617362693 created "2017-06-05" @default.
• W2617362693 creator A5059192605 @default.
• W2617362693 date "1961-01-01" @default.
• W2617362693 modified "2023-10-16" @default.
• W2617362693 title "THE HAEM–GLOBIN LINKAGE" @default.
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• W2617362693 doi "https://doi.org/10.1016/b978-1-4831-9646-6.50017-x" @default.
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