A click chemistry approach to site-specific immobilization of a small laccase enables efficient direct electron transfer in a biocathode

Dongli Guan; Yadagiri Kurra; Wenshe Liu; Zhilei Chen

doi:10.1039/c4cc09179e

A click chemistry approach to site-specific immobilization of a small laccase enables efficient direct electron transfer in a biocathode

Chem Commun (Camb). 2015 Feb 14;51(13):2522-5. doi: 10.1039/c4cc09179e.

Authors

Dongli Guan¹, Yadagiri Kurra, Wenshe Liu, Zhilei Chen

Affiliation

¹ Chemical Engineering Department, Texas A&M University, College Station, TX 77843, USA.

PMID: 25566975
DOI: 10.1039/c4cc09179e

Abstract

Controlled orientation of a small laccase on a multi-walled carbon nanotube electrode was achieved via copper-free click chemistry mediated immobilization. Modification of the enzyme was limited to only the tethering site and involved the genetic incorporation of the unnatural amino acid 4-azido-L-phenylalanine (AzF). This approach enabled efficient direct electron transfer.

MeSH terms

Azides / chemistry
Azides / metabolism
Click Chemistry*
Electrodes
Electron Transport
Enzymes, Immobilized / chemistry*
Enzymes, Immobilized / metabolism
Laccase / chemistry*
Laccase / metabolism
Nanotubes, Carbon / chemistry
Phenylalanine / analogs & derivatives
Phenylalanine / chemistry
Phenylalanine / metabolism

Substances

Azides
Enzymes, Immobilized
Nanotubes, Carbon
4-azidophenylalanine
Phenylalanine
Laccase