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Using a combination of CW-EPR X-band spectroscopy and DFT calculations, we show that the active site of a chitin-active AA10 lytic polysaccharide monooxygenase can exist in three different protonation states, representing the ionisation of the coordinating groups.

Mapping the protonation states of the histidine brace in an AA10 lytic polysaccharide monooxygenase using CW-EPR spectroscopy and DFT calculations