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Inside Cover
Inside Cover: Precise Design of Artificial Cofactors for Enhancing Peroxidase Activity of Myoglobin: Myoglobin Mutant H64D Reconstituted with a “Single-Winged Cofactor” Is Equivalent to Native Horseradish Peroxidase in Oxidation Activity (Chem. Asian J. 9/2011)
Article first published online: 9 AUG 2011
DOI: 10.1002/asia.201190036
Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Matsuo, T., Fukumoto, K., Watanabe, T. and Hayashi, T. (2011), Inside Cover: Precise Design of Artificial Cofactors for Enhancing Peroxidase Activity of Myoglobin: Myoglobin Mutant H64D Reconstituted with a “Single-Winged Cofactor” Is Equivalent to Native Horseradish Peroxidase in Oxidation Activity (Chem. Asian J. 9/2011). Chem. Asian J., 6: 2182. doi: 10.1002/asia.201190036
Publication History
- Issue published online: 9 AUG 2011
- Article first published online: 9 AUG 2011
- Abstract
- Cited By
Keywords:
- cofactors;
- heme proteins;
- myoglobin;
- oxidation;
- reconstitution
Single-winged heme co-factor brings about the drastic enhancement of the catalytic oxidation activity in myoglobin, an oxygen-storage protein. In their Full Paper on page 2491 ff, Matsuo, Hayashi et al. propose a versatile strategy to alter or enhance the functions of naturally occurring hemoproteins using a combination of “genetic mutation” and the “introduction of a synthetic co-factor”. This synergistic strategy develops unique proteins with ultra-native functions.