Design and structure analysis of artificial metalloproteins:: Selective coordination of his64 to copper complexes with square-planar structure in the apo-myoglobin scaffold

Design and structure analysis of artificial metalloproteins:: Selective coordination of his64 to copper complexes with square-planar structure in the apo-myoglobin scaffold
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DOI:
10.1021/ic070289m
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发表时间:
2007-06-25
影响因子:
4.6
通讯作者:
Watanabe, Yoshihito
Watanabe, Yoshihito
中科院分区:
化学2区
文献类型:
--
作者:
Abe, Satoshi;Ueno, Takafumi;Watanabe, Yoshihito

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载脂蛋白-肌红蛋白(apo-Mb)由三种铜配合物组成:铜-II(SA-Phe)(1;SA-Phe=N-水杨叉-L-苯丙氨酸)、铜-II(SA-亮氨酸)(2;SA-亮氨酸=N-水杨叉-L-亮氨酸)和铜-II(SA-Ala)(3;SA-Ala=N-水杨叉-L-丙氨酸)。1(.)apo-Mb(1.65埃分辨率)和2(.)apo-Mb(1.8埃分辨率)的晶体结构表明,apo-Mb中的Cu-II原子周围的配位几何构型是扭曲的方形平面,在apo-Mb空腔中有一个三齿的Sal-X和一个His64的N-epsilon原子,这些铜配合物的平面与血红素的平面垂直。这些结果表明apo-Mb腔可以容纳具有不同配位几何构型的金属络合物。
apo-Myoglobin (apo-Mb) was reconstituted with three copper complexes: Cu-II(Sal-Phe) (1; Sal-Phe = N-salicylidene-L-phenylalanato), Cu-II(Sal-Leu) (2; Sal-Leu = N-salicylidene-L-leucinato), and Cu-II(Sal-Ala) (3; Sal-Ala = N-salicylidene-L-alanato). The crystal structures of 1(.)apo-Mb (1.65 angstrom resolution) and 2(.)apo-Mb (1.8 angstrom resolution) show that the coordination geometry around the Cu-II atom in apo-Mb is distorted square-planar with tridentate Sal-X and a N-epsilon atom of His64 in the apo-Mb cavity and the plane of these copper complexes is perpendicular to that of heme. These results suggest that the apo-Mb cavity can hold metal complexes with various coordination geometries.