By comparing the ground-state electron density based Hirshfeld population of the complete model system and its components, some intriguing informations about the fractional electron transfers at the non-covalent interfaces has been revealed. The hydrogen bond formation between Cys52(S -) and the Arg266(H) promotes a transfer of an amount of 0.283e -(fig. ) from the electron-rich Heme moiety to the α-helix 8 . The detailed investigation of the Hirshfeld population (table 1) confirms that most of the electron densities are depleted from the porphyrin macrocycle (table in SI). On the other end of the communication pathway, PLP losses 0.786e -population. Most importantly, the delocalization enhances the small positive charge at the electrophilic C4A atom (table 1 and table ). As the ease of addition of a nucleophile to the C4A atom is directly de- pendent on the electrophlic character of that center, the increased positive charge at C4A atom will definitely promote the neucleophilic attack. Thus, disruption of these interactions alter the π-electron configuration at the enzyme active site resulting in diminished enzymatic activity as observed by mutations at the hydrogen bonded aa residues. These findings are further verified using Löwdin population analysis (table ). For understanding the effect of different hCBS conformations on the electronic redistribution, we have further investigated two other models obtained from two different crystal structures; viz. 4PCU and 1M54. The atomic charge densities along with the key hydrogen bond distances for different conformation has been tabulated in the table 1. For 1M54, the orientations of the -OH group of Thr257 and Thr260 aa residues are changed. The reorientation makes the -OH groups inaccessible for the formation of hydrogen bond with PLP phosphate group. Consequently in the 1M54 model, lesser amount of electron is gained by the α-helix 8 from PLP as compared to the other hCBS crystal structures. For this model, we have observed significant decrease of the positive charge at the C4A atom (table 1 and table ) which contradicts the other models. We have further investigated the effect of inter-molecular distances between the components of the communication pathways by analysing electron redistribution at different snapshots of the simulated trajectory (see Fig. and table ) from our previous work. These results clearly indicate that a stronger association at the hydrogen bonding sites results in larger delocalization of the π-electrons. From the above discussion it is now quite clear that the α-helix 8 accepts the fractional electrons from both the highly π-conjugated ends. This implies that the α-helix 8 is not only a merely structural bridge between the Heme and PLP, it also acts as an electron reservoir in the communication pathways present between the distant cofactors of the hCBS.