期刊
CHEMISTRY-A EUROPEAN JOURNAL
卷 26, 期 22, 页码 4974-4979出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.201905598
关键词
bioelectrocatalysis; copper efflux oxidase; electron transfer; oxygen reduction reaction; site-saturation mutagenesis
资金
- Alexander von Humboldt Foundation
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.
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