The recent discovery of the first rare-earth dependent methanol dehydrogenase (MDH) has brought this family of metals into the field of bioinorganic chemistry.1 In the enzyme’s crystal structure the Ca2+ ion, ubiquitous in MDH enzymes, had been replaced by the lanthanide ion Ce3+. The enzyme was identified to use a pyrroloquinoline quinone (PQQ) cofactor to catalyze the dehydrogenation of methanol to formaldehyde and formic acid, a distinct advantage over the Ca2+ system, which only produces formaldehyde, and at a slower rate. The rare earth cations La-Gd were all competent at growing the bacteria. Toward understanding and exploiting the reactions catalyzed by this unique system we have developed a series of organic soluble cofactor surrogates. These surrogates have been used as ligands for rare-earth cations to model the active site of the MDH enzyme. The reactivity of these complexes was also explored; a summary of the results of these first studies in the bioinorganic chemistry of the rare earth metals will be disclosed. (1) Pol, A.; Barends, T. R. M.; Dietl, A.; Khadem, A. F.; Eygensteyn, J.; Jetten, M. S. M.; Op den Camp, H. J. M. Environ. Microbiol. 2014, 16, 255.

Biologically (RE)levant metals: Model studies of a new rare-earth dependent methanol dehydrogenase

251st National Meeting (2016)

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