Rau H K, DeJonge N, Haehnel W
Institut für Biologie II/Biochemie, Albert-Ludwigs-Universität Freiburg, Schänzlestrasse 1, D-79104 Freiburg, Germany.
Proc Natl Acad Sci U S A. 1998 Sep 29;95(20):11526-31. doi: 10.1073/pnas.95.20.11526.
The design and chemical synthesis of two de novo four-helix bundle proteins is described; each protein has two bound cofactors. Their construction from purified peptides is based on the modular assembly of different amphiphilic helices by chemoselective coupling to a cyclic peptide template. In the hydrophobic interior of the antiparallel four-helix bundle these proteins contain a heme in a binding pocket with two ligating histidine residues. A ruthenium-tris(bipyridine) complex is covalently bound to different positions at the hydrophilic side of one of the heme-binding helices. Laser-induced electron transfer across the varied distance through this helix has been studied and compared with a pathway analysis. The UV-visible, CD, and mass spectra are consistent with the structure and orientation predetermined by the template.
描述了两种从头设计的四螺旋束蛋白的设计和化学合成；每种蛋白都有两个结合的辅因子。它们由纯化的肽构建而成，基于通过化学选择性偶联到环状肽模板上对不同两亲性螺旋进行模块化组装。在反平行四螺旋束的疏水内部，这些蛋白在一个结合口袋中含有一个血红素，带有两个配位组氨酸残基。一个钌-三联吡啶配合物共价结合到血红素结合螺旋之一的亲水侧的不同位置。研究了通过该螺旋在不同距离上的激光诱导电子转移，并与路径分析进行了比较。紫外可见光谱、圆二色光谱和质谱与模板预先确定的结构和取向一致。
