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- Title
Mutational dissection of a hole hopping route in a lytic polysaccharide monooxygenase (LPMO).
- Authors
Ayuso-Fernández, Iván; Emrich-Mills, Tom Z.; Haak, Julia; Golten, Ole; Hall, Kelsi R.; Schwaiger, Lorenz; Moe, Trond S.; Stepnov, Anton A.; Ludwig, Roland; Cutsail III, George E.; Sørlie, Morten; Kjendseth Røhr, Åsmund; Eijsink, Vincent G. H.
- 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. Lytic polysaccharide monooxygenases (LPMOs) are mono copper enzymes with outstanding industrial applicability. Here, the authors investigate the "hole hopping" mechanism in a bacterial LPMO and show that a strictly conserved tryptophan is critical for radical formation and hole transference, as well as reveal a correlation between the efficiency of hole transference and enzyme performance under oxidative stress.
- Subjects
POLYSACCHARIDES; COPPER enzymes; MONOOXYGENASES; RADICALS (Chemistry); INDUSTRIAL capacity; TRYPTOPHAN; HISTIDINE
- Publication
Nature Communications, 2024, Vol 15, Issue 1, p1
- ISSN
2041-1723
- Publication type
Article
- DOI
10.1038/s41467-024-48245-w