The Library
Structural and functional characterisation of multi-copper oxidase CueO from lignin-degrading bacterium Ochrobactrum sp. reveal its activity towards lignin model compounds and lignosulfonate
Tools
Granja-Travez, R. S., Wilkinson, Rachael C., Persinoti, G. F., Squina, F. M., Fülöp, Vilmos and Bugg, Tim (2018) Structural and functional characterisation of multi-copper oxidase CueO from lignin-degrading bacterium Ochrobactrum sp. reveal its activity towards lignin model compounds and lignosulfonate. FEBS Journal, 285 (9). pp. 1684-1700. doi:10.1111/febs.14437 ISSN 1742-4658.
|
PDF
WRAP-structural-functional-characterisation-multi-copper-oxidase-Bugg-2018.pdf - Accepted Version - Requires a PDF viewer. Download (2336Kb) | Preview |
Official URL: https://doi.org/10.1111/febs.14437
Abstract
The identification of enzymes responsible for oxidation of lignin in lignin‐degrading bacteria is of interest for biotechnological valorization of lignin to renewable chemical products. The genome sequences of two lignin‐degrading bacteria, Ochrobactrum sp., and Paenibacillus sp., contain no B‐type DyP peroxidases implicated in lignin degradation in other bacteria, but contain putative multicopper oxidase genes. Multi‐copper oxidase CueO from Ochrobactrum sp. was expressed and reconstituted as a recombinant laccase‐like enzyme, and kinetically characterized. Ochrobactrum CueO shows activity for oxidation of β‐aryl ether and biphenyl lignin dimer model compounds, generating oxidized dimeric products, and shows activity for oxidation of Ca‐lignosulfonate, generating vanillic acid as a low molecular weight product. The crystal structure of Ochrobactrum CueO (OcCueO) has been determined at 1.1 Å resolution (PDB: 6EVG), showing a four‐coordinate mononuclear type I copper center with ligands His495, His434 and Cys490 with Met500 as an axial ligand, similar to that of Escherichia coli CueO and bacterial azurin proteins, whereas fungal laccase enzymes contain a three‐coordinate type I copper metal center. A trinuclear type 2/3 copper cluster was modeled into the active site, showing similar structure to E. coli CueO and fungal laccases, and three solvent channels leading to the active site. Site‐directed mutagenesis was carried out on amino acid residues found in the solvent channels, indicating the importance for residues Asp102, Gly103, Arg221, Arg223, and Asp462 for catalytic activity. The work identifies a new bacterial multicopper enzyme with activity for lignin oxidation, and implicates a role for bacterial laccase‐like multicopper oxidases in some lignin‐degrading bacteria.
Item Type: | Journal Article | ||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Subjects: | Q Science > QK Botany T Technology > TP Chemical technology |
||||||||||||||||||
Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) |
||||||||||||||||||
Library of Congress Subject Headings (LCSH): | Lignin -- Research, Lignosulfonates, Biotechnology, Bacteria | ||||||||||||||||||
Journal or Publication Title: | FEBS Journal | ||||||||||||||||||
Publisher: | Blackwell | ||||||||||||||||||
ISSN: | 1742-4658 | ||||||||||||||||||
Official Date: | May 2018 | ||||||||||||||||||
Dates: |
|
||||||||||||||||||
Volume: | 285 | ||||||||||||||||||
Number: | 9 | ||||||||||||||||||
Page Range: | pp. 1684-1700 | ||||||||||||||||||
DOI: | 10.1111/febs.14437 | ||||||||||||||||||
Status: | Peer Reviewed | ||||||||||||||||||
Publication Status: | Published | ||||||||||||||||||
Access rights to Published version: | Restricted or Subscription Access | ||||||||||||||||||
Date of first compliant deposit: | 23 March 2018 | ||||||||||||||||||
Date of first compliant Open Access: | 25 March 2019 | ||||||||||||||||||
RIOXX Funder/Project Grant: |
|
||||||||||||||||||
Related URLs: |
Request changes or add full text files to a record
Repository staff actions (login required)
View Item |
Downloads
Downloads per month over past year