9I1U

Lytic polysaccharide monooxygenase from Cellvibrio japonicus - CjAA10B

Summary for 9I1U

• Entry DOI: 10.2210/pdb9i1u/pdb
• Descriptor: Chitin binding protein, putative, cbp33/10B, COPPER (II) ION, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: lytic polysaccharide monooxygenase, cellulose., oxidoreductase
• Biological source: Cellvibrio japonicus
• Total number of polymer chains: 8
• Total formula weight: 192796.92

Authors

Branch, J.,Hemsworth, G.R. (deposition date: 2025-01-17, release date: 2025-12-24, Last modification date: 2026-03-04)

Primary citation

Reid, E.K.,Miles, C.G.,Lloyd-Laney, H.O.,Nairn, A.K.,Branch, J.,Garland, N.,Yates, N.D.J.,Ascham, A.,Walton, P.H.,Hemsworth, G.,Parkin, A.
Electrochemical Insight into the Copper Redox Chemistry and H 2 O 2 and O 2 Reducing Capability of Two AA10 Lytic Polysaccharide Monooxygenases.
Acs Electrochem, 2:239-257, 2026

PubMed Abstract: Lytic polysaccharide monooxygenases ([L]-PMOs) are copper-containing enzymes that catalyse cleavage of the glycosidic bond, a process central to microbial biomass degradation. Here, we describe electrochemical methods used to investigate the Cu redox chemistry and the polysaccharide-free catalytic activity of two AA10 LPMOs: AA10B from and AA10 from . Immobilisation of these enzymes on the surface of a graphite electrode allows for direct electrochemical measurements of Cu redox cycling as well as the ability of both LPMOs to reduce HO vs O. These measurements can be advantageous when compared to biological dye assays as they provide direct kinetic measurements and allow for investigation over a wider range of environmental conditions. Values of and - are reported for HO and O reduction by AA10B and AA10 from pH 5-7, with AA10 consistently outperforming AA10B. Both enzymes perform faster catalysis with HO but when comparing the affinity-coupled specificity constant ( / ), the LPMOs perform similarly with both HO and O, suggesting both substrates are viable. We also note an increase in redox signals as pH is decreased that correlates with EPR data suggesting a second species is formed PubMed: 41669087
DOI: 10.1021/acselectrochem.5c00266

Experimental method

X-RAY DIFFRACTION (1.9 Å)