(560in) An Investigation into the Catalytic Cycle of Cytochrome P-450 Involving 1-n-Alkyl-3-Methylimidazolium Cations As Substrate
AIChE Annual Meeting
2019
2019 AIChE Annual Meeting
Catalysis and Reaction Engineering Division
Poster Session: Catalysis and Reaction Engineering (CRE) Division
Wednesday, November 13, 2019 - 3:30pm to 5:00pm
Cytochrome P-450 has been identified and widely studied for their role in oxidation of a wide variety of molecules in aerobic and anaerobic environments. Thus, it was deemed necessary to capture the effects of the cytochromeâs active site molecule on imidazolium-based ([Cnmim]+) cations to develop a computational framework for their biodegradability. For this, the enzymatic center of the P-450 molecule (heme) was modeled as an iron porphyrin molecule with an Fe-based center conjugated with the amino acid residue cysteine (FePCys) at its proximal side. The cations were included in the model as a potential substrate for the P-450 enzyme in complexation with the underlying porphyrin molecule. This interaction was modeled using DFT calculations by adapting a purely quantum mechanical framework at the M06 level of theory. To include the conformational effects, two different conformations of the ionic liquid cation, namely, tail up and tail down conformations, were considered in this work varying the 1-n-alkyl chain on the cation progressively along the homologous series (n =2,4,6,8,10). To provide insight into the dynamics of the substrate while binding to the active site molecule (FePCys) and further, different steps of the catalytic cycle were modeled using a synchronous approach. Result and discussion would describe the energetics and properties evaluated from the interaction between FePCys and ionic liquid cation from the binding, reduction and subsequent dioxygen insertion processes in the cycle. Also, key analysis of the interaction strength and thermodynamics of the system derived from each step would be included to provide further insight into the protein-ligand model.