Design and Structure Analysis of Artificial Metalloproteins: Selective Coordination of His64 to Copper Complexes with Square-Planar Structure in the apo-Myoglobin ScaffoldClick to copy article linkArticle link copied!
- Satoshi Abe
- Takafumi Ueno
- Pattubala A. N. Reddy
- Seiji Okazaki
- Tatsuo Hikage
- Atsuo Suzuki
- Takashi Yamane
- Hiroshi Nakajima
- Yoshihito Watanabe
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 Å resolution) and 2·apo-Mb (1.8 Å resolution) show that the coordination geometry around the CuII atom in apo-Mb is distorted square-planar with tridentate Sal-X and a Nε 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.
†
Department of Chemistry, Graduate School of Science, Nagoya University.
‡
PRESTO, Japan Science and Technology Agency (JST), Japan.
§
Department of Biotechnology, Graduate School of Engineering, Nagoya University.
‖
High Intensity X-ray Diffraction Laboratory, Nagoya University.
*
To whom correspondence should be addressed. E-mail: yoshi@ nucc.cc.nagoya-u.ac.jp. Phone: +81-52-789-3049. Fax: +81-52-789-2953.
⊥
Research Center for Materials Science, Nagoya University.
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