Tuning the geometries of a de novo blue copper protein by axial interactions
Tuning the geometries of a de novo blue copper protein by axial interactions
复制标题
通过轴向相互作用调整从头蓝铜蛋白的几何形状
DOI：
10.1007/s00775-012-0916-x
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发表时间：
2012
影响因子：
3
通讯作者：
Takashi Ogura and Toshiki Tanaka
中科院分区：
文献类型：
--
作者：
Daigo Shiga;Yusuke Hamano;Misato Kamei;Yasuhiro Funahashi;Hideki Masuda;Miyuki Sakaguchi;Takashi Ogura and Toshiki Tanaka
1型铜蛋白中Cu2+的轴向相互作用控制着蛋白质的物理特性。我们调整了重新设计的具有四螺旋束结构的蓝铜蛋白的几何形状。设计的蛋白质轴向结合各种配体，如氯化物、磷酸盐、硫酸盐、醋酸盐、叠氮化物和咪唑，与Cu2+结合，呈现蓝色或绿色。紫外可见光谱在600 nm和450 nm左右，theA~450/A~600比值在0.14 ~ 1.58之间。较强的轴向相互作用使1型铜位点的几何形状从三角形平面几何（蓝色铜）转变为四面体形状（绿色铜）。共振拉曼光谱分析表明，磷酸盐结合型具有最高强度的Cu-S键，与质体青素相似。氯结合型表现出与星青花苷和亚硝酸盐还原酶相似的特征，咪唑结合型表现出与azurin M121E突变体相似的特征。
The axial interactions of Cu2+in type 1 copper proteins control the physical characteristics of the proteins. We tuned the geometries of a de novo designed blue copper protein with a four-helical bundle structure. The designed protein axially bound various ligands, such as chloride, phosphate, sulfate, acetate, azide, and imidazole, to Cu2+, exhibiting a blue or green color. The UV–vis spectral bands were observed at approximately 600 nm and approximately 450 nm, with theA~450/A~600ratios between 0.14 and 1.58. The stronger axial interaction shifted the geometry of the type 1 copper site from trigonal planar geometry (blue copper) toward a tetrahedral-like geometry (green copper). Resonance Raman spectral analyses showed that the phosphate-bound type had the highest-strength Cu–S bond, similar to that of plastocyanin. The chloride-bound type exhibited features similar to those of stellacyanin and nitrite reductase, and the imidazole-bound type exhibited features similar to those of azurin M121E mutant.