Final answer:
The incoming dNTP acts as the nucleophile in the DNA polymerase reaction, attacking the alpha-phosphorous to form a new phosphodiester bond in the presence of divalent metal ions.
Step-by-step explanation:
The nucleophilic attacker in the DNA polymerase mechanism of action is the incoming dNTP (deoxynucleotide triphosphate). During DNA synthesis, the enzyme DNA polymerase utilizes a template strand to form a new complementary strand. The current growing chain of DNA provides a 3'-OH group which acts as a nucleophile. This nucleophile attacks the alpha-phosphorous atom of the incoming dNTP. The reaction is a nucleophilic substitution where the release of pyrophosphate (PP) occurs, facilitating the formation of the new phosphodiester bond.
To catalyze the formation of the phosphodiester bond, divalent metal ions, typically Mg2+, are necessary. This metal ion is crucial for proper positioning and stability of the nucleophilic 3'-OH group as well as the incoming dNTP.
DNA polymerase requires a primer to begin DNA synthesis, and this primer can be an RNA primer synthesized by a primase. However, the primer itself does not act as the nucleophile; rather, the nucleophile is the 3'-OH group that comes from the primer or the previous nucleotide in the growing DNA chain.