Enhancement of Peroxygenase Activity of Horse Heart Myoglobin by Modification of Heme-propionate Side Chains
Author:
Publisher
The Chemical Society of Japan
Subject
General Chemistry
Reference15 articles.
1. Investigations of the Roles of the Distal Heme Environment and the Proximal Heme Iron Ligand in Peroxide Activation by Heme Enzymes via Molecular Engineering of Myoglobin
2. Engineering Novel Metalloproteins: Design of Metal-Binding Sites into Native Protein Scaffolds
3. The roles of His-64, Tyr-103, Tyr-146, and Tyr-151 in the epoxidation of styrene and beta-methylstyrene by recombinant sperm whale myoglobin.
4. Preparation and Reactions of Myoglobin Mutants Bearing both Proximal Cysteine Ligand and Hydrophobic Distal Cavity: Protein Models for the Active Site of P-450
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1. Rational Heme Protein Design: All Roads Lead to Rome;Chemistry – An Asian Journal;2013-05-23
2. Generation of Functionalized Biomolecules using Hemoprotein Matrices with Small Protein Cavities for Incorporation of Cofactors;Coordination Chemistry in Protein Cages;2013-04-02
3. 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;Chemistry - An Asian Journal;2011-06-09
4. A Biomimetic Copper Corrole - Preparation, Characterization, and Reconstitution with Horse Heart Apomyoglobin;Zeitschrift für anorganische und allgemeine Chemie;2010-05-04
5. Enantioselective Synthesis of Sulfoxides: 2000−2009;Chemical Reviews;2010-04-23
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