Modification of the heme distal side in myoglobin by cyanogen bromide. Heme environmental structures and ligand binding properties of the modified myoglobin.
Modification of the heme distal side in myoglobin by cyanogen bromide. Heme environmental structures and ligand binding properties of the modified myoglobin.
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溴化氰对肌红蛋白中血红素远端的修饰。
DOI：
10.1021/bi00316a010
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发表时间：
1984
期刊：
影响因子：
2.9
通讯作者：
I. Morishima
中科院分区：
文献类型：
--
作者：
Y. Shiro;I. Morishima
肌红蛋白 (Mb) 的甲硫氨酸、脱氧和 CO 形式与化学计量的溴化氰 (BrCN) 发生反应，导致 1H NMR、光吸收和红外光谱发生显着变化。这些光谱变化被解释为由血红素环境的实质性改变引起，最有可能是由于血红素远端组氨酸残基的修饰。研究还表明，修饰后的 Mb 不会与一些外源配体（如 CN-、CH3NH2 和 O2）结合，尽管它与 N-3 或 CO 结合。这些独特的配体结合特性也与远端组氨酸通过氢键稳定配位配体的作用以及空间约束进行了讨论。
Met, deoxy, and CO forms of myoglobin (Mb) react with a stoichiometric amount of cyanogen bromide (BrCN) to cause substantial changes in the 1H NMR, optical absorption, and infrared spectra. These spectral changes were interpreted as arising from the substantial alterations in the heme environments, most probably due to the modification of the histidine residue at the heme distal side. It is also revealed that the modified Mb does not combine with some exogenous ligands such as CN-, CH3NH2, and O2, although it does with N-3 or CO. These unique ligand binding properties are also discussed with relevance to a role of the distal histidine in stabilizing the coordinated ligand through a hydrogen bond and to a steric constraint.
异腈-血红素蛋白复合物的质子核磁共振研究。
DOI：
--
发表时间：
1983
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Mims,MP;Olson,JS;Russu,IM;Miura,S;Cedel,TE;Ho,C
通讯作者：
Ho,C
钴肌红蛋白和血红蛋白的研究。
DOI：
--
发表时间：
1981
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Ikeda-Saito,M;Hori,H;Inubushi,T;Yonetani,T
通讯作者：
Yonetani,T