In this computational study, we explore the mechanism of both reaction steps associated with the experiments performed by Zare and co-workers. Our calculations reveal that OEEFs indeed have a strong catalytic effect on both ribose phosphorylation and subsequent nucleoside formation. Interestingly, the key aspects of the uncovered mechanism, as well as the inferred anomeric selectivity, are in close resemblance to the enzymatic mechanism of phosphorolysis performed by purine or pyrimidine nucleoside phosphorylases confirming that OEEFs also ought to play an important role in enzymatic catalysis. On the methodological side, we demonstrate that strong electric fields can radically reshuffle the conformer stability order of flexible molecules, such as ribose and its derivatives. As such, a rigorous treatment of conformational space, both in the presence and absence of electric fields, is essential to ensure the selection of representative conformers, and hence the construction of meaningful reaction profiles.