title: A click chemistry approach to site-specific immobilization of a small laccase enables efficient direct electron transfer in a biocathode.
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.
authors.affiliation: Chemical Engineering Department, Texas A&M University, College Station, TX 77843, USA.
authors.forename: Dongli
authors.initials: D
authors.lastname: Guan
authors.forename: Yadagiri
authors.initials: Y
authors.lastname: Kurra
authors.forename: Wenshe
authors.initials: W
authors.lastname: Liu
authors.forename: Zhilei
authors.initials: Z
authors.lastname: Chen
mesh_terms: D001386:Azides / Q000737:chemistry / Q000378:metabolism; D057930:Click Chemistry; D004566:Electrodes; D004579:Electron Transport; D004800:Enzymes, Immobilized / Q000737:chemistry* / Q000378:metabolism; D042845:Laccase / Q000737:chemistry* / Q000378:metabolism; D037742:Nanotubes, Carbon / Q000737:chemistry; D010649:Phenylalanine / Q000031:analogs & derivatives / Q000737:chemistry / Q000378:metabolism
chemical_list: D001386:Azides; D004800:Enzymes, Immobilized; D037742:Nanotubes, Carbon; C027162:4-azidophenylalanine; D010649:Phenylalanine; D042845:Laccase