NMR Studies of Monoliganded Fe-Co Hybrid Hemoglobins: Their Quaternary Structure and Proximal Histidine Coordination

Toshiro Inubushi, Cynthia D’Ambrosio, Masao Ikeda-Saito, Takashi Yonetani

研究成果: Article査読

22 被引用数 (Scopus)

抄録

Tricobalt-substituted Fe-Co hybrid hemoglobins have been synthesized by cross-linking symmetric Fe-Co hybrid HbA and Co-substituted mutant HbC (β6 Glu-Lys) with bis(3, 5-dibromosalicyl) fumarate. Carbon monoxy derivatives of these molecules can serve as important models of monoliganded hemoglobins, the intermediate species produced in the First step of oxygen binding to hemoglobin. Acceptance of the first ligand in an a subunit gave essentially no change in the proximal histidine coordination in the remaining deoxy subunits and a small alteration of deoxy quaternary structure. However, when the first ligand was bound to a 0 subunit, significant change in the proximal histidine coordination and complete elimination of one hydrogen bond in the deoxy quaternary structure occurred. Such substantial differences in the structures of the two monoliganded hemoglobins obtained by NMR allow us to postulate the possible course of oxygen binding. Also, the observation of asynchronous decreases in the intensities of so-called “T-state” markers and the absence of concomitant increases in the so-called ”R-state” marker indicate the existence of more than two quaternary structures for Hb and contradict the two-state allosteric theory.

本文言語English
ページ(範囲)3799-3803
ページ数5
ジャーナルJournal of the American Chemical Society
108
13
DOI
出版ステータスPublished - 1986 1 1

ASJC Scopus subject areas

  • 触媒
  • 化学 (全般)
  • 生化学
  • コロイド化学および表面化学

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