ミオグロビンの機能と遠位残基の役割

概要

論文の詳細を見る
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 not explained 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.
日本生物物理学会の論文
1994-01-25