Site-specific incorporation of a redox-active amino acid into proteins
Site-specific incorporation of a redox-active amino acid into proteins
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DOI：
10.1021/ja038242x
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发表时间：
2003-12-03
影响因子：
15
通讯作者：
Schultz, PG
中科院分区：
文献类型：
--
作者：
Alfonta, L;Zhang, ZW;Schultz, PG
氧化还原活性氨基酸 3,4-二羟基-L-苯丙氨酸 (DHP) 可以进行双电子氧化成醌，在大肠杆菌对 TAG 密码子的响应中，它已被选择性且有效地掺入蛋白质中。我们已经证明 DHP 可以在蛋白质内被电化学氧化。将氧化还原活性氨基酸位点特异性地整合到蛋白质中的能力应该有助于蛋白质中电子转移的研究，并使得能够设计具有新特性的氧化还原蛋白质。
The redox-active amino acid 3,4-dihydroxy-l-phenylalanine (DHP), which can undergo two-electron oxidation to a quinone, has been incorporated selectively and efficiently into proteins inEscherichiacoliin response to a TAG codon. We have demonstrated that DHP can be oxidized electrochemically within the protein. The ability to incorporate a redox-active amino acid site specifically into proteins should facilitate the study of electron transfer in proteins, as well as enable the engineering of redox proteins with novel properties.