甲烷单加氧酶双铁位点存在两个组氨酸配体的证据。
Evidence for two histidine ligands at the diiron site of methane monooxygenase.
作者信息
Smith D D, Dalton H
机构信息
Department of Biological Sciences, University of Warwick, Coventry, England.
出版信息
Eur J Biochem. 1992 Dec 1;210(2):629-33. doi: 10.1111/j.1432-1033.1992.tb17463.x.
Circular dichroism spectroscopy has shown the hydroxylase component of methane monooxygenase to have a high helical content. The apoprotein has the same secondary structure as the holoenzyme. Chemical modification shows 12 histidines to be reactive with diethylpyrocarbonate in the holoenzyme, whereas 14 are reactive in the apoenzyme. Two histidine residues are implicated as iron ligands. Further chemical modification results suggest a cysteine residue is in close proximity to the diiron centre.
圆二色光谱显示，甲烷单加氧酶的羟化酶组分具有很高的螺旋含量。脱辅基蛋白与全酶具有相同的二级结构。化学修饰表明，全酶中有12个组氨酸可与焦碳酸二乙酯发生反应，而脱辅酶中有14个组氨酸具有反应活性。有两个组氨酸残基被认为是铁配体。进一步的化学修饰结果表明，有一个半胱氨酸残基靠近双铁中心。
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