An artificial di-iron oxo-protein with phenol oxidase activity
An artificial di-iron oxo-protein with phenol oxidase activity
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DOI：
10.1038/nchembio.257
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发表时间：
2009-12-01
影响因子：
14.8
通讯作者：
Lombardi, Angela
中科院分区：
文献类型：
--
作者：
Faiella, Marina;Andreozzi, Concetta;Lombardi, Angela
在这里，我们报告的从头设计和NMR结构的四螺旋束二铁蛋白的酚氧化酶活性。辅因子结合位点和酚结合位点的引入需要掺入对蛋白质折叠自由能有害的残基。然而，通过优化远离活性位点的环的序列获得足够的稳定性。
Here we report the de novo design and NMR structure of a four-helical bundle di-iron protein with phenol oxidase activity. The introduction of the cofactor-binding and phenol-binding sites required the incorporation of residues that were detrimental to the free energy of folding of the protein. Sufficient stability was, however, obtained by optimizing the sequence of a loop distant from the active site.