人工金属蛋白的设计与结构分析：在脱辅基肌红蛋白支架中His64与具有平面正方形结构的铜配合物的选择性配位

Design and structure analysis of artificial metalloproteins: selective coordination of His64 to copper complexes with square-planar structure in the apo-myoglobin scaffold.

作者信息

Abe Satoshi, Ueno Takafumi, Reddy Pattubala A N, Okazaki Seiji, Hikage Tatsuo, Suzuki Atsuo, Yamane Takashi, Nakajima Hiroshi, Watanabe Yoshihito

机构信息

Department of Chemistry, Graduate School of Science, Nagoya University, Nagoya 464-8602, Japan.

出版信息

Inorg Chem. 2007 Jun 25;46(13):5137-9. doi: 10.1021/ic070289m. Epub 2007 May 25.

DOI:10.1021/ic070289m

PMID:17523632

Abstract

apo-Myoglobin (apo-Mb) was reconstituted with three copper complexes: CuII(Sal-Phe) (1; Sal-Phe = N-salicylidene-L-phenylalanato), CuII(Sal-Leu) (2; Sal-Leu = N-salicylidene-L-leucinato), and CuII(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 CuII atom in apo-Mb is distorted square-planar with tridentate Sal-X and a Nepsilon 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.

摘要

脱辅基肌红蛋白（apo-Mb）与三种铜配合物进行了重构：CuII(Sal-Phe)（1；Sal-Phe = N-水杨醛亚基-L-苯丙氨酸）、CuII(Sal-Leu)（2；Sal-Leu = N-水杨醛亚基-L-亮氨酸）和CuII(Sal-Ala)（3；Sal-Ala = N-水杨醛亚基-L-丙氨酸）。1.apo-Mb（分辨率为1.65埃）和2.apo-Mb（分辨率为1.8埃）的晶体结构表明，apo-Mb中CuII原子周围的配位几何形状为扭曲的平面正方形，由三齿的Sal-X和apo-Mb腔中His64的一个Nε原子配位，并且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腔可以容纳具有各种配位几何形状的金属配合物。