Contribution of O2 Binding Cooperativity and the Bohr Effect to Efficient Oxygen Uptake and Transport by Mammalian Hemoglobin: A New Look in the Model Protein

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  • ZHANG Yan
    Department of Bioinformatics, Harbin Medical University, China
  • IMAI Kiyohiro
    Deparment of Frontier Bioscience, Faculty of Engineering, Hosei University
  • KOBAYASHI Michiyori
    Department of Biology, Faculty of Science, Niigata University

Bibliographic Information

Other Title
  • 哺乳類ヘモグロビンの協同作用とボーア効果は協調して酸素の獲得と輸送を行っている　―規範タンパク質における新たな視点―
  • ホニュウルイ ヘモグロビン ノ キョウドウ サヨウ ト ボーア コウカ ワ キョウチョウシテ サンソ ノ カクトク ト ユソウ オ オコナッテイル キハン タンパクシツ ニ オケル アラタナ シテン

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Description

The slope of the oxygen equilibrium curve (OEC) of mammalian-hemoglobin (Hb) is maximized at S (oxygen saturation) value of 0.38, and the slope of the S vs. P/P50 (P is partial oxygen pressure; P50 is P at S = 1/2) plot at a P/P50 value of 1 is one-forth that of the Hill-coefficient (n). OECs of mammalian Hbs are designed to have an identical optimal P50 value for O2 delivery and the effectiveness of the Bohr shift (shift of OEC upon pH changes) at O2 loading site. This fact is favorable for uptake and delivery of maximum amount of O2 for fetal blood. To have the identical optimal P50 value for O2 delivery and for the efficiency of the Bohr shift, the relationship, PaO2/PvO2 = ((n + 1)/(n − 1))2/n, is required to hold, where PaO2 and PvO2 are P for arterial and venous bloods, respectively.<br>

Journal

  • Seibutsu Butsuri

    Seibutsu Butsuri 47 (3), 167-173, 2007

    The Biophysical Society of Japan General Incorporated Association

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