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- [2] The Reaction of Synechocystis Catalase–Peroxidase (KatG) with Isoniazid Investigated by Multifrequency (9–285 GHz) EPR Spectroscopy Applied Magnetic Resonance, 2010, 37 : 267 - 277
- [3] Distinct Role of Specific Tryptophans in Facilitating Electron Transfer or as [Fe(IV)=O Trp•] Intermediates in the Peroxidase Reaction of Bulkholderia pseudomallei Catalase-Peroxidase: A Multifrequency EPR Spectroscopy Investigation JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2009, 131 (24) : 8557 - 8563
- [4] Multifrequency (9-285 GHz) EPR spectroscopy as a selective tool to unequivocally identify and characterize the reactivity of tryptophan radicals as the alternative [Fe(IV)=O TrpR.] intermediates in mono and bi-functional heme peroxidases and related heme enzymes ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 2011, 241
- [5] Selective substrate reactivity of [Fe(IV)=O Trp•] in heme enzymes: implications for M-tuberculosis KatG-mediated activation of isoniazid prodrug JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY, 2014, 19 : S217 - S217
- [6] A remarkable peroxidase-like behavior of the catalase KatA from the pathogenic bacteria Helicobacter pylori: The oxidation reaction with formate as substrate and the stabilization of an [Fe(IV) = O Trp•] intermediate assessed by multifrequency EPR spectroscopy JOURNAL OF INORGANIC BIOCHEMISTRY, 2024, 257