Functional variation among <scp>LPMOs</scp> revealed by the inhibitory effects of cyanide and buffer ions

Enzymes known as lytic polysaccharide monooxygenases (LPMOs) are mono-copper polysaccharide-degrading peroxygenases that engage in several on- and off-pathway redox reactions involving O<sub>2</sub> and H<sub>2</sub>O<sub>2</sub>. Herein, we show that the known metalloenzyme inhibitor cyanide inhibits reductive activation of LPMOs by binding to the LPMO-Cu(II) state and that the degree of inhibition depends on the concentrations of the polysaccharide substrate, the reductant and H<sub>2</sub>O<sub>2</sub>. Importantly, this analysis revealed differences between fungal NcAA9C and bacterial SmAA10A, which have different secondary copper coordination spheres. These differences were also highlighted by the observation that phosphate, a commonly used buffer ion, strongly inhibits NcAA9C while not affecting reactions with SmAA10A. The results provide insight into LPMO inhibition and catalysis and highlight pitfalls in the analysis thereof.

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Publication Details

Journal
FEBS Letters
Published
2025-02-06
DOI
https://doi.org/10.1002/1873-3468.15105
Citations
1
Primary Topic
Cassava research and cyanide
Type
article
Field-Weighted Citation Impact
1.75

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article

Functional variation among LPMOs revealed by the inhibitory effects of cyanide and buffer ions

Zarah Forsberg, Åsmund K. Røhr, Lorenz Schwaiger, Roland Ludwig et al.
1 citations
FEBS Letters
Cassava research and cyanide
1.75
article

Functional variation among LPMOs revealed by the inhibitory effects of cyanide and buffer ions

Zarah Forsberg, Åsmund K. Røhr, Lorenz Schwaiger, Roland Ludwig, Vincent G. H. Eijsink, Anton A. Stepnov, Ole Golten, Iván Ayuso‐Fernández, Kelsi R. Hall, Tom Z. Emrich‐Mills, Morten Sørlie
article en
1 citations

Abstract

Enzymes known as lytic polysaccharide monooxygenases (LPMOs) are mono-copper polysaccharide-degrading peroxygenases that engage in several on- and off-pathway redox reactions involving O<sub>2</sub> and H<sub>2</sub>O<sub>2</sub>. Herein, we show that the known metalloenzyme inhibitor cyanide inhibits reductive activation of LPMOs by binding to the LPMO-Cu(II) state and that the degree of inhibition depends on the concentrations of the polysaccharide substrate, the reductant and H<sub>2</sub>O<sub>2</sub>. Importantly, this analysis revealed differences between fungal NcAA9C and bacterial SmAA10A, which have different secondary copper coordination spheres. These differences were also highlighted by the observation that phosphate, a commonly used buffer ion, strongly inhibits NcAA9C while not affecting reactions with SmAA10A. The results provide insight into LPMO inhibition and catalysis and highlight pitfalls in the analysis thereof.

FEBS LettersVol. 599(9)
University of Canterbury (NZ), Centro de Investigaciones Biológicas Margarita Salas (ES), Norwegian University of Life Sciences (NO), BOKU University (AT)
Austrian Science Fund, H2020 European Research Council
Clean water and sanitation
Openalex Percentile: Top 17%
Cassava research and cyanide
1.75
DOIOpen Access PDFOpenAlex
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