From a periplasmic pyrroloquinoline quinone (PQQ) binding protein, we report the generation of metal-binding capabilities and resultant activity. Installing the metal-binding site adjacent to the redox-active PQQ moiety, the organic cofactor becomes a coenzyme and participates in biocatalytic functionality. Through a combination of spectroscopic, structural, computational, and biochemical investigations, we report on the unique structural and functional properties of this new artificial metalloenzyme platform. These studies range from modelling and mechanistic investigation of La3+-dependent alcohol dehydrogenation reaction to examining dynamic pathways for electron transfer and substrate access to the active site. Activity correlations relating to metal ion speciation and the resultant novel modes of reactivity will be presented.