Lanthanide–induced conformational change of methanol dehydrogenase involving coordination change of cofactor pyrroloquinoline quinone

There is emerging interests to the role of lanthanides as cofactor in XoxF-type methanol dehydrogenase (MHD). Here, classical molecular dynamics simulations combined with fragment molecular orbital calculations were employed to rationalize enzymatic activities of MHD (both XoxF- and MxaF- types) carrying different lanthanides. In XoxF–type MDH, lanthanide binding to cofactor pyrroloquinoline quinone was found to switch from tridentate to unidentate fashion as it switches from lighter to heavier lanthanide. This fact possibly plays crucial role to the enzymatic activity exclusive to XoxF–type MDH incorporating lighter lanthanides.