Traditionally, the mechanism of enzymatic catalysis has often been explained by the "induced fit" model, but this model struggles to fully account for its exponential catalytic efficiency. This paper proposes a new mechanism: proteases can be viewed as a kind of molecular nuclear magnetic resonance system, where Hu207a or metal ions reversibly coordinate with amino groups, generating an induced electric field, which in turn triggers the formation of an alternating electromagnetic field in the α-helix structure and interacts with the static magnetic field produced by the β-sheet structure. At specific carboxyl groups (with bond characteristics), nuclear magnetic resonance of hydrogen atoms or electrons is excited, thereby generating microwave radiation locally. This microwave promotes the dissociation of substrates into highly reactive free radicals or ions, greatly accelerating the reaction rate. This paper combines quantum tunneling effects with microwave catalysis theory to provide a new physical explanation for the high efficiency of enzyme-catalyzed reactions.