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43 results
  • Tension in haemoglobin revealed by Fe-His(F8) bond rupture in the fully liganded T-state. [Journal Article]
    J Mol Biol 1997; 271(2):161-7Paoli M, Dodson G, … Wilkinson AJ
  • In 1972, Perutz proposed that the low affinity of T-state haemoglobin is caused by tension in the bond between the iron and the proximal histidine, restraining the Fe from moving into the porphyrin plane on binding oxygen. This proposal has often been disputed. If such tension does exist, it will be manifest in the liganded T-state. Here we describe the structure of the fully liganded T-state cya…
  • Asymmetric hemoglobin hybrids. [Journal Article]
    J Mol Biol 1996; 263(1):90-7Marden MC, Griffon N, Poyart C
  • We have investigated the functional properties of hemoglobin (Hb) valency hybrids, and specifically whether it makes a difference if the oxidized subunits are on the same dimer (asymmetric hybrid) or not. CO recombination kinetics were used to probe the allosteric equilibrium of tetramers with two oxidized subunits. Asymmetric hybrids were prepared by mixing HbCO with a large excess of cyano-metH…
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