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• W115556960 abstract "A number of redox reactions involving the interconversion of the iron(II) and iron(III) forms of oxygen-carrying proteins will be discussed. Such studies are important in understanding the loss of oxygen-carrying ability of the protein (by autoxidation) and the conversion of met back into deoxy-form which is continually occurring in normal erythrocytes. (A) Reduction of a large number of metmyoglobin-ligand adducts, Mb + L, by dithionite has been examined. For L = CN − , imidazole (and derivatives), and pyridine (and derivatives) direct attack of SO 2 − on the coordinated ligand is suggested, followed by electron transfer through the π system to the metal ion. For all other adducts, reduction occurs through the dissociated fragment Mb + OH 2 formed by ligand dissociation from Mb + L. (B) An extensive study of the conversion of oxyhemerythrin into met in the presence of anions shows parallelisms with that of oxyhemoglobin (Caughey et al.) in several respects. Reaction rates are first order in the oxy-form, anion and proton. A similar nucleophilicity order for effect of anions is observed. However, unlike oxyhemoglobin, CNO − and N 3 − bleach the oxyhemerythrin color by forming anion adducts with deoxyhemerythrin." @default.
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• W115556960 date "1978-01-01" @default.
• W115556960 modified "2023-09-27" @default.
• W115556960 title "REDOX SYSTEM: IRON(II)-IRON(III) INTERCONVERSION IN OXYGEN-CARRYING PROTEINS11This work was supported by National Institutes of Health, Division of Blood Diseases and Resources, to whom we are very grateful." @default.
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• W115556960 doi "https://doi.org/10.1016/b978-0-12-164350-8.50037-6" @default.
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