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Preparation of Artificial Metalloenzymes by Insertion of Chromium(III) Schiff Base Complexes into Apomyoglobin Mutants

Authors


  • 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.

Abstract

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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.

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