This work was supported by a Grant-in-Aid for Scientific Research 11490036 and 1122828 (to Y.W.), 13740384 (to T.U.). We also thank Prof. T. Yamane, Prof. A. Suzuki, and Mr. M. Kono at Nagoya University for valuable guidance and help with the X-ray crystallographic analysis.
Preparation of Artificial Metalloenzymes by Insertion of Chromium(III) Schiff Base Complexes into Apomyoglobin Mutants†
Article first published online: 26 FEB 2003
© 2002 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 42, Issue 9, pages 1005–1008, March 3, 2003
How to Cite
Ohashi, M., Koshiyama, T., Ueno, T., Yanase, M., Fujii, H. and Watanabe, Y. (2003), Preparation of Artificial Metalloenzymes by Insertion of Chromium(III) Schiff Base Complexes into Apomyoglobin Mutants. Angew. Chem. Int. Ed., 42: 1005–1008. doi: 10.1002/anie.200390256
- Issue published online: 26 FEB 2003
- Article first published online: 26 FEB 2003
- Manuscript Revised: 19 NOV 2002
- Manuscript Received: 15 JUL 2002
- asymmetric catalysis;
- protein modifications;
- Schiff bases
Insertion of a symmetric metal complex, [CrIII(5,5′-tBu-salophen)]+ (H2salophen=N,N′-bis(salicylidene)-1,2-phenylenediamine), into the active site of apomyoglobin is demonstrated (see picture). The metal ion and the ligand structure are very important factors that influence the binding affinity of the metal complex with the myoglobin (Mb) cavity. Semisynthetic metalloenzymes can catalyze enantioselective sulfoxidation by using the chiral protein cavity.