Controlled depolymerization of cellulose by light-driven lytic polysaccharide oxygenases
Bastien Bissaro,
Eirik Kommedal,
Åsmund K. Røhr and
Vincent G. H. Eijsink ()
Additional contact information
Bastien Bissaro: Norwegian University of Life Sciences (NMBU)
Eirik Kommedal: Norwegian University of Life Sciences (NMBU)
Åsmund K. Røhr: Norwegian University of Life Sciences (NMBU)
Vincent G. H. Eijsink: Norwegian University of Life Sciences (NMBU)
Nature Communications, 2020, vol. 11, issue 1, 1-12
Abstract:
Abstract Lytic polysaccharide (mono)oxygenases (LPMOs) perform oxidative cleavage of polysaccharides, and are key enzymes in biomass processing and the global carbon cycle. It has been shown that LPMO reactions may be driven by light, using photosynthetic pigments or photocatalysts, but the mechanism behind this highly attractive catalytic route remains unknown. Here, prompted by the discovery that LPMOs catalyze a peroxygenase reaction more efficiently than a monooxygenase reaction, we revisit these light-driven systems, using an LPMO from Streptomyces coelicolor (ScAA10C) as model cellulolytic enzyme. By using coupled enzymatic assays, we show that H2O2 is produced and necessary for efficient light-driven activity of ScAA10C. Importantly, this activity is achieved without addition of reducing agents and proportional to the light intensity. Overall, the results highlight the importance of controlling fluxes of reactive oxygen species in LPMO reactions and demonstrate the feasibility of light-driven, tunable enzymatic peroxygenation to degrade recalcitrant polysaccharides.
Date: 2020
References: Add references at CitEc
Citations: View citations in EconPapers (1)
Downloads: (external link)
https://www.nature.com/articles/s41467-020-14744-9 Abstract (text/html)
Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.
Export reference: BibTeX
RIS (EndNote, ProCite, RefMan)
HTML/Text
Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14744-9
Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/
DOI: 10.1038/s41467-020-14744-9
Access Statistics for this article
Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie
More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().