Rapid and Oriented Immobilization of Laccases on Electrodes via a Methionine-Rich Peptide
Citations Over TimeTop 10% of 2021 papers
Abstract
Different from other laccases, copper efflux oxidase (CueO) from Escherichia coli possesses an additional methionine-rich segment (MetRich), which is generally considered to be detrimental to its oxidase activity. Herein, we reveal that MetRich plays an important role in rapid immobilization of CueO on electrodes by studying the adsorption and bioelectrocatalysis behaviors of CueO, a truncated CueO (ΔMetRich CueO), and a serine-rich substituted CueO (SerRich CueO). Atomic molecular dynamics (MD) simulations demonstrate that the synergistic effect of π–π stacking and hydrophobic interactions contribute to the high affinity of MetRich to carbon nanotubes. Considering that the location of the electron acceptor (i.e., T1 Cu active site) in the family of laccases is close to the C-terminus, MetRich fused to another bacterial laccase, spore coat protein A (CotA) from Bacillus licheniformics, is found to endow CotA with the properties of rapid and oriented adsorption at the electrode surface. The finding and validation make MetRich a valuable binding motif for the rapid immobilization and high performance of laccases and perhaps other oxidoreductases in bioelectrocatalytic applications.
Related Papers
- → Characterization of a laccase-like multicopper oxidase from newly isolated Streptomyces sp. C1 in agricultural waste compost and enzymatic decolorization of azo dyes(2013)71 cited
- → Production of extracellular laccase from the newly isolated Bacillus sp. PK4(2016)49 cited
- → Characterization of a novel high-pH-tolerant laccase-like multicopper oxidase and its sequence diversity in Thioalkalivibrio sp(2015)33 cited
- → Identification and Characterization of a Novel Plasmid-Encoded Laccase-Like Multicopper Oxidase from Ochrobactrum sp. BF15 Isolated from an On-Farm Bio-Purification System(2021)6 cited