Metalloenzymes catalyze various biological reactions with high efficiency owing to their well-defined metal centers. However, alterations in their expression, downregulation, and their naiveness in industrial conditions restrict their operation. Thus, the pursuit of artificial metalloenzymes represents ever-growing research in biotechnology. Molecular dynamics (MD) simulations have emerged as a critical tool in the design, optimization, and understanding of natural metalloenzymes providing unparalleled insights into their dynamic behaviors at an atomistic level. The technique sheds light on structural behaviors of metal centers, their interaction with the rest of the protein, coordination dynamics of metal ions, and the structural design of enzyme mimics. MD simulations have been utilized in proteins over a decade now. Advancements in parametrization of metal centers, more realistic water models, and updated algorithms and tools to understand the dynamics of metal-containing proteins boosted the computational studies for design of artificial metalloenzymes. This chapter explores pivotal role of MD studies in the development of artificial metalloenzymes, focusing on how computational approaches can guide the design of metalloproteins with tailored properties. The chapter focuses on the applications of MD simulations based on four distinct strategies to mimic an enzyme, then proceeds with theoretical advancements to lead realistic simulations, and concludes with the outlook.