Conformational state andtransformation in Mn(II) and Mn(III) hemoglobins and azide Mn(III) hemoglobin

Plese, C.F.; Amma, E. L.; Rodesiler, P. F.

doi:10.1016/s0006-291x(77)80054-5

Cited by 9 publications

(1 citation statement)

References 15 publications

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“…CD studies of human Hb in the visible, Soret, and near-UV regions have revealed alteration of optical activity of the heme group and aromatic amino acid residues owing to both the changes of the tertiary structure of polypeptide chains and the quaternary structural transition. [1][2][3][4] Hb A shows a pronounced change of the CD spectra at the 280∼300 nm upon the T→R transition. T-state Hb (de-oxyHb A) exhibits a distinct negative CD band.…”

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Contribution of ?140Tyr and ?37Trp to the near-UV CD spectra on quaternary structure transition of human hemoglobin A

Nagai

2000

Chirality

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The CD band of human adult hemoglobin (Hb A) at 280 ∼ 290 nm shows a pronounced change from a small positive band to a definite negative band on the oxy (R) to deoxy (T) structural transition. This change has been suggested to be due to environmental alteration of Tyrs (α42, α140, and β145) or β37 Trp residues located at the α1β2 subunit interface by deoxygenation. In order to evaluate contributions of α140Tyr and β37Trp to this change of CD band, we compared the CD spectra of two mutant Hbs, Hb Rouen (α140Tyr→His) and Hb Hirose (β37Trp→Ser) with those of Hb A. Both mutant Hbs gave a distinct, but smaller negative CD band at 287nm in the deoxy form than that of deoxyHb A. Contributions of α140Tyr and β37Trp to the negative band at the 280 ∼ 290 nm region were estimated from difference spectra to be 30% and 26%, respectively. These results indicate that the other aromatic amino acid residues, α42Tyr and β145Tyr, at the α1β2 interface, are also responsible for the change of the CD band upon the R→T transition of Hb A. Chirality 12:216–220, 2000. © 2000 Wiley‐Liss, Inc.

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confidence: 99%