Projects per year
Abstract
Myoglobin (Mb) can react with hydrogen peroxide (H 2O 2) 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 variants with iron chlorin e6 (Fe−Ce6) and manganese chlorin e6 (Mn−Ce6) cofactors were found to have improved catalytic efficiency for both guaiacol and TCP substrates in comparison with wild-type Mb, i. e. Fe-protoporphyrin IX-Mb. Furthermore, the selected cofactors were incorporated into the scaffold of a Mb mutant, swMb H64D. Enhanced peroxidase activity for both substrates were found via the reconstitution of Fe−Ce6 into the mutant scaffold.
Original language | English |
---|---|
Article number | e202200197 |
Number of pages | 10 |
Journal | Chembiochem |
Volume | 23 |
Issue number | 18 |
Early online date | 11 Jul 2022 |
DOIs | |
Publication status | Published - 16 Sep 2022 |
Keywords
- peroxidase activity
- myoglobin variants
- reconstituted
- artificial cofactors
Fingerprint
Dive into the research topics of 'Peroxidase activity of myoglobin variants reconstituted with artificial cofactors'. Together they form a unique fingerprint.Projects
- 2 Active
-
Intracellular Controlled Radical Polymerizations
EPSRC (Engineering and Physical Sciences Research Council)
1/04/21 → 31/03/23
Project: Research