Abstract
AbstractIt has been a long‐standing goal for chemists to develop selective catalytic oxidation systems with molecular oxygen as a green terminal oxidant from the inspiration of active sites in natural metalloenzymes. Lanthanide‐centered methanol dehydrogenase (Ln‐MDH), which contains the same pyrroloquinoline quinone (PQQ) redox cofactor as the analogous calcium‐based MDH (Ca‐MDH) and exhibits good reactivity in alcohol oxidation, was discovered in 2011 and aroused extensive research interest during the past decade. In this review, we present the progress in the bioinorganic and biomimetic chemistry of the metal‐PQQ‐MDH that includes (1) an introduction of the structure, synthesis, and property of the coenzyme PQQ, the metal‐PQQ active sites, the two commonly believed mechanisms of alcohol oxidation, and the insights from computation chemistry; (2) representative structures and the alcohol oxidation mechanism of Ca‐MDH inspired transition‐metal models from an earlier time to around 2000; (3) the developments in the ligand modifications, coordination chemistry, and catalytic alcohol oxidation of the model systems of Ln‐MDH from 2011 to June 2024; and (4) other biological or chemical metal‐PQQ‐like systems and the applications in broader fields. Finally, the challenge and opportunity in the bioinspired catalytic oxidation systems, as well as the clarification of the enzymatic mechanism, were mentioned.
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