Mutational dissection of a hole hopping route in a lytic polysaccharide monooxygenase (LPMO)

Iván Ayuso-Fernández (), Tom Z. Emrich-Mills, Julia Haak, Ole Golten, Kelsi R. Hall, Lorenz Schwaiger, Trond S. Moe, Anton A. Stepnov, Roland Ludwig, George E. Cutsail, Morten Sørlie, Åsmund Kjendseth Røhr and Vincent G. H. Eijsink ()
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Iván Ayuso-Fernández: Norwegian University of Life Sciences (NMBU)
Tom Z. Emrich-Mills: Norwegian University of Life Sciences (NMBU)
Julia Haak: Max Planck Institute for Chemical Energy Conversion
Ole Golten: Norwegian University of Life Sciences (NMBU)
Kelsi R. Hall: Norwegian University of Life Sciences (NMBU)
Lorenz Schwaiger: University of Natural Resources and Life Sciences (BOKU)
Trond S. Moe: Norwegian University of Life Sciences (NMBU)
Anton A. Stepnov: Norwegian University of Life Sciences (NMBU)
Roland Ludwig: University of Natural Resources and Life Sciences (BOKU)
George E. Cutsail: Max Planck Institute for Chemical Energy Conversion
Morten Sørlie: Norwegian University of Life Sciences (NMBU)
Åsmund Kjendseth Røhr: Norwegian University of Life Sciences (NMBU)
Vincent G. H. Eijsink: Norwegian University of Life Sciences (NMBU)

Nature Communications, 2024, vol. 15, issue 1, 1-15

Abstract: Abstract Oxidoreductases have evolved tyrosine/tryptophan pathways that channel highly oxidizing holes away from the active site to avoid damage. Here we dissect such a pathway in a bacterial LPMO, member of a widespread family of C-H bond activating enzymes with outstanding industrial potential. We show that a strictly conserved tryptophan is critical for radical formation and hole transference and that holes traverse the protein to reach a tyrosine-histidine pair in the protein’s surface. Real-time monitoring of radical formation reveals a clear correlation between the efficiency of hole transference and enzyme performance under oxidative stress. Residues involved in this pathway vary considerably between natural LPMOs, which could reflect adaptation to different ecological niches. Importantly, we show that enzyme activity is increased in a variant with slower radical transference, providing experimental evidence for a previously postulated trade-off between activity and redox robustness.

Date: 2024
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DOI: 10.1038/s41467-024-48245-w

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