Peroxidase Activity of Myoglobin Variants Reconstituted with Artificial Cofactors.

ABSTRACT: Myoglobin (Mb) can react with hydrogen peroxide (H₂ O₂ ) to form a highly active intermediate compound and catalyse oxidation reactions. To enhance this activity, known as pseudo-peroxidase activity, previous studies have focused on the modification of key amino acid residues of Mb or the heme cofactor. In this work, the Mb scaffold (apo-Mb) was systematically reconstituted with a set of cofactors based on six metal ions and two ligands. These Mb variants were fully characterised by UV-Vis spectroscopy, circular dichroism (CD) spectroscopy, inductively coupled plasma mass spectrometry (ICP-MS) and native mass spectrometry (nMS). The steady-state kinetics of guaiacol oxidation and 2,4,6-trichlorophenol (TCP) dehalogenation catalysed by Mb variants were determined. Mb v

SUBMITTER: Guo C 

PROVIDER: S-EPMC9545363 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature