Journal
CHEMISTRY-A EUROPEAN JOURNAL
Volume 26, Issue 22, Pages 4974-4979Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.201905598
Keywords
bioelectrocatalysis; copper efflux oxidase; electron transfer; oxygen reduction reaction; site-saturation mutagenesis
Categories
Funding
- Alexander von Humboldt Foundation
Ask authors/readers for more resources
Copper efflux oxidase (CueO) from Escherichia coli is a special bacterial laccase due to its fifth copper binding site. Herein, it is discovered that the fifth Cu occupancy plays a crucial and favorable role of electron relay in bioelectrocatalytic oxygen reduction. By substituting the residues at the four coordinated positions of the fifth Cu, 11 beneficial variants are identified with >= 2.5-fold increased currents at -250 mV (up to 6.13 mA cm(-2)). Detailed electrocatalytic characterization suggests the microenvironment of the fifth Cu binding site governs the electrocatalytic current of CueO. Additionally, further electron transfer analysis assisted by molecular dynamics (MD) simulation demonstrates that an increase in localized structural stability and a decrease of distance between the fifth Cu and the T1 Cu are two main factors contributing to the improved kinetics of CueO variants. It may guide a novel way to tailor laccases and perhaps other oxidoreductases for bioelectrocatalytic applications.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available