Contreras A, Drummond M
AFRC Institute of Plant Sciences Research, Nitrogen Fixation Laboratory, Uiversity of Sussex, Brighton, U.K.
Gene. 1991 Jul 15;103(1):83-6. doi: 10.1016/0378-1119(91)90395-r.
The sequence Cys184-Ala-Asp-Cys187 in the NifL protein of Klebsiella pneumoniae, for which a role in oxygen sensing and/or metal binding has been proposed, was altered by introducing two mutations, Cys184----Ala and Cys187----Ala, using oligodeoxyribonucleotide-directed mutagenesis. Neither mutation abolished ammonium or oxygen control of nif transcription, although some impairment of function was apparent. The two Cys residues are therefore unlikely to have a direct role in oxygen sensing or metal binding, but probably make some contribution to protein folding or stability.
肺炎克雷伯菌固氮调节蛋白NifL中Cys184 - Ala - Asp - Cys187序列，有人提出其在氧感应和/或金属结合中起作用，通过使用寡聚脱氧核糖核苷酸定向诱变引入两个突变（Cys184→Ala和Cys187→Ala）对其进行了改变。尽管功能有一些明显的损害，但这两个突变都没有消除对固氮基因转录的铵或氧调控。因此，这两个半胱氨酸残基不太可能在氧感应或金属结合中起直接作用，但可能对蛋白质折叠或稳定性有一定贡献。
