1J3F

Crystal Structure of an Artificial Metalloprotein:Cr(III)(3,3'-Me2-salophen)/apo-A71G Myoglobin

1J3F の概要

• エントリーDOI: 10.2210/pdb1j3f/pdb
• 分子名称: Myoglobin, CHROMIUM ION, PHOSPHATE ION, ... (5 entities in total)
• 機能のキーワード: myoglobin, asymmetric catalysis, crystal, schiff bases, chromium, oxygen storage-transport complex, oxygen storage/transport
• 由来する生物種: Physeter catodon (sperm whale)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18318.35

構造登録者

Koshiyama, T.,Kono, M.,Ohashi, M.,Ueno, T.,Suzuki, A.,Yamane, T.,Watanabe, Y. (登録日: 2003-01-24, 公開日: 2004-05-18, 最終更新日: 2023-10-25)

主引用文献

Ueno, T.,Koshiyama, T.,Ohashi, M.,Kondo, K.,Kono, M.,Suzuki, A.,Yamane, T.,Watanabe, Y.
Coordinated Design of Cofactor and Active Site Structures in Development of New Protein Catalysts
J.Am.Chem.Soc., 127:6556-6562, 2005

PubMed Abstract: New methods for the synthesis of artificial metalloenzymes are important for the construction of novel biocatalysts and biomaterials. Recently, we reported new methodology for the synthesis of artificial metalloenzymes by reconstituting apo-myoglobin with metal complexes (Ohashi, M. et al., Angew Chem., Int. Ed. 2003, 42, 1005-1008). However, it has been difficult to improve their reactivity, since their crystal structures were not available. In this article, we report the crystal structures of M(III)(Schiff base).apo-A71GMbs (M = Cr and Mn). The structures suggest that the position of the metal complex in apo-Mb is regulated by (i) noncovalent interaction between the ligand and surrounding peptides and (ii) the ligation of the metal ion to proximal histidine (His93). In addition, it is proposed that specific interactions of Ile107 with 3- and 3'-substituent groups on the salen ligand control the location of the Schiff base ligand in the active site. On the basis of these results, we have successfully controlled the enantioselectivity in the sulfoxidation of thioanisole by changing the size of substituents at the 3 and 3' positions. This is the first example of an enantioselective enzymatic reaction regulated by the design of metal complex in the protein active site.

PubMed: 15869276
DOI: 10.1021/ja045995q

実験手法

X-RAY DIFFRACTION (1.45 Å)