Having expanded NCB candidate space, we aimed to understand the stability in terms of the NCB decomposition mechanism. NCBs which have been studied experimentally are noted to have high decomposition rates in phosphate buffer, which is problematic for CFB applications where enzymes often have highest activity in phosphate buffers. Thus, we modeled the decomposition mechanism of NCBs using a negatively charged phosphate molecule to approximate the buffer solution. Referencing a previously-proposed decomposition scheme, we modeled the decomposition of four NCBs which have experimental decomposition rates in phosphate buffer: MNAH (A1a), BNAH (F1a), P2NAH (G1a), and P3NAH (H1a). The activation barriers obtained are consistent with a process that is kinetically feasible at ambient temperatures.