Site-Directed Mutagenesis of Multicopper Oxidase from Hyperthermophilic Archaea for High-Voltage Biofuel Cells.
Biocathode
Biofuel cell
Multicopper oxidase
Redox potential
Site-directed mutagenesis
Journal
Applied biochemistry and biotechnology
ISSN: 1559-0291
Titre abrégé: Appl Biochem Biotechnol
Pays: United States
ID NLM: 8208561
Informations de publication
Date de publication:
Feb 2021
Feb 2021
Historique:
received:
15
04
2020
accepted:
29
09
2020
pubmed:
8
10
2020
medline:
1
6
2021
entrez:
7
10
2020
Statut:
ppublish
Résumé
Enzymes from hyperthermophilic archaea are potential candidates for industrial use because of their superior pH, thermal, and long-term stability, and are expected to improve the long-term stability of biofuel cells (BFCs). However, the reported multicopper oxidase (MCO) from hyperthermophilic archaea has lower redox potential than MCOs from other organisms, which leads to a decrease in the cell voltage of BFCs. In this study, we attempted to positively shift the redox potential of the MCO from hyperthermophilic archaeon Pyrobaculum aerophilum (McoP). Mutations (M470L and M470F) were introduced into the axial ligand of the T1 copper atom of McoP, and the enzymatic chemistry and redox potentials were compared with that of the parent (M470). The redox potentials of M470L and M470F shifted positively by about 0.07 V compared with that of M470. In addition, the catalytic activity of the mutants towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) increased 1.2-1.3-fold. The thermal stability of the mutants and the electrocatalytic performance for O
Identifiants
pubmed: 33025566
doi: 10.1007/s12010-020-03440-5
pii: 10.1007/s12010-020-03440-5
doi:
Substances chimiques
Archaeal Proteins
0
Oxidoreductases
EC 1.-
copper oxidase
EC 1.16.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
492-501Références
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