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• W1551228722 endingPage "111" @default.
• W1551228722 startingPage "101" @default.
• W1551228722 abstract "The proton nuclear magnetic resonance spectra of human adult deoxyhemoglobin and several mutant or modified deoxyhemoglobins taken in 0.1 m-deuterated sodium phosphate at pD 7 and 25 °C show three prominent hyperfine shifted lines at approximately −18, −12 and −7 p.p.m. from HDO. In deoxyhemoglobins with amino acid substitutions or modifications near the heme group of the β chain, such as Hb Zurich (β63 His → Arg), Hb F3 (β → γ), carboxypeptidase A-treated Hb A, and spin-labeled Hb A, the position of the lowest field resonance line is variable but the two high-field lines are unshifted. In those hemoglobins with substitutions in the α1 − β2 subunit contact region of the protein, such as Hb Chesapeake (α92 Arg → Leu), Hb J Capetown (α92 Arg → Gln), Hb Yakima (β99 Asp → His), and Hb Kempsey (β99 Asp → Asn), all three resonance lines show simultaneous variations in their positions, regardless of which chain is abnormal. The lowest two field lines are assigned to heme methyl groups, and it is proposed that the heme groups in deoxyhemoglobin are non-equivalent. Since the lowest field line is sensitive to modification in the β chain, it is assigned to a methyl group of the β heme. The invariant line at about −12 p.p.m. is assigned to a homologous methyl of the α heme. The simultaneous variation of the spectral lines in hemoglobins with altered subunit contacts is interpreted to mean that an amino acid substitution in this region of the molecule perturbs not only the heme in the mutant chain but also the heme in the adjacent chain. This result suggests that in normal hemoglobin, the unliganded hemes may be influenced by the state of ligation of the hemes in the contiguous chains." @default.
• W1551228722 created "2016-06-24" @default.
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• W1551228722 date "1971-08-01" @default.
• W1551228722 modified "2023-09-26" @default.
• W1551228722 title "Nuclear magnetic resonance studies of hemoglobins" @default.
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• W1551228722 doi "https://doi.org/10.1016/0022-2836(71)90450-5" @default.
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