In Vitro Heme Coordination of a Dye-Decolorizing Peroxidase-The Interplay of Key Amino Acids, pH, Buffer and Glycerol.
UV-vis spectroscopy
active site structure
alkaline transition
electron paramagnetic resonance
glassing agents
heme peroxidases
ligand binding
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
12 Sep 2021
12 Sep 2021
Historique:
received:
30
06
2021
revised:
31
08
2021
accepted:
03
09
2021
entrez:
28
9
2021
pubmed:
29
9
2021
medline:
25
2
2023
Statut:
epublish
Résumé
Dye-decolorizing peroxidases (DyPs) have gained interest for their ability to oxidize anthraquinone-derived dyes and lignin model compounds. Spectroscopic techniques, such as electron paramagnetic resonance and optical absorption spectroscopy, provide main tools to study how the enzymatic function is linked to the heme-pocket architecture, provided the experimental conditions are carefully chosen. Here, these techniques are used to investigate the effect of active site perturbations on the structure of ferric P-class DyP from
Identifiants
pubmed: 34576013
pii: ijms22189849
doi: 10.3390/ijms22189849
pmc: PMC8468270
pii:
doi:
Substances chimiques
Amino Acids
0
Bacterial Proteins
0
Heme
42VZT0U6YR
Peroxidase
EC 1.11.1.7
Glycerol
PDC6A3C0OX
Types de publication
Evaluation Study
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Research Foundation Flanders / Austrian Science Fund - FWO/FWF lead agency grant
ID : G005416N
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