Our previous paper (J. Phys. Chem. A 2005, 109, 7606) using computed atomic charges, based on the quantum theory of atoms in molecules (QTAIM), on azolium models of thiamin diphosphate has shown that only sulfur acts as an effective electron sink in the formation of the thiamin carbanion intermediate. Herein we apply natural bond orbital (NBO) theory to the analysis of orbital contributions to canonical molecular orbitals (CMOs) of six abbreviated azolium analogs of the carbanion to better understand the unique function of sulfur. The NBO/CMO data provide a description of the origin of the first thiamin electron sink: sulfur performing in the sigma- and pi-orbitals of the transition state as well as in the carbanion, and its advantages due to low electronegativity and moderate size. At the next level of thiamin modeling, we include the six-membered pyrimidine ring to represent the prerequisite V-structure in the iminopyrimidine tautomeric form. This model is subjected to incremental deprotonation and MO decomposition. The 4'-pyrimidylimine moiety, in addition to being an internal base to abstract the C2 proton, also performs as the second electron sink. Thus, the LUMOs of the thiazolium and pyrimidylimine systems working in tandem stabilize the developing charges in these transient structures, with facilitation from their HOMOs. Further, the absence of detectable amounts of the C2 carbanion in (13)C2-labeled thiamin-enzyme complex by NMR is explained. Both NBO analysis and the QTAIM topological electronic properties suggest the operation of a H-bonding scheme that leads to the formation of a cryptic C2 carbanion that is not accumulated. The shielding of the carbanion by the N4'-H hydrogen bond is weakened by N1'-H deprotonation. Consequently, prior return of the N1' proton to the nearby glutamate may be the switch for streaming a timed-release of the unstable C2 carbanion to the incoming substrate.