Functional properties of the pseudo-distal residue in the mollusc myoglobin.
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- YAMAMOTO Yasuhiko
- Department of Chemistry. University of Tsukuba
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- INOUE Yoshio
- Department of Biomolecular Engineering, Tokyo Institute of Technology
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- CHÛJOÔ Riichirô
- Department of Material Engineering, Nishi-Tokyo Universitv
Bibliographic Information
- Other Title
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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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Description
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
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- Seibutsu Butsuri
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Seibutsu Butsuri 34 (1), 25-32, 1994
The Biophysical Society of Japan General Incorporated Association
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Keywords
Details 詳細情報について
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- CRID
- 1390001206532532736
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- NII Article ID
- 110001157337
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- NII Book ID
- AN00129693
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- ISSN
- 13474219
- 05824052
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- NDL BIB ID
- 3868114
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed