Functional properties of the pseudo-distal residue in the mollusc myoglobin.

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  • ミオグロビンの機能と遠位残基の役割
  • ミオグロビン ノ キノウ ト エンイ ザンキ ノ ヤクワリ

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Abstract

The mollusc myoglobin possesses naturally occurring substitution at the distal E7 position (Val-E7) and its oxygen affinity is only slightly lower than those of the common mammalian myoglobins possessing the usual His E7. The structure-function relationship in this myoglobin is notexplained on the basis of the results obtained from the study of the site-directed mutation at the E7 position of mammalian myoglobin. The recent mutation, crystallographic and nuclear magnetic resonance spectroscopy studies have revealed that a guanidino NH proton of Arg E10 in the mollusc myoglobin serves as an alternative hydrogen-bond donor to the bound ligand to maintain a high ligand affinity. The functional properties of the mollusc myoglobin possessing the Val E7 are controlled by a mechanism different from that of the mammalian myoglobin possessing His E7.

Journal

  • Seibutsu Butsuri

    Seibutsu Butsuri 34 (1), 25-32, 1994

    The Biophysical Society of Japan General Incorporated Association

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