Computational Study on Docking of Laccase and Cyanide-Bridged Ag-Cu Complex for Designing the Improved Biofuel Cell Cathode
Abstract
The extrinsic catalytic properties of the laccase enzyme enable it to oxidize a wide range of metallic compounds, making it an essential enzyme for producing biofuel. We have employed computational and experimental approaches while searching cathode materials for biofuel cells composed of laccase and various metal complexes. Laccase is an oxygen-reducing copper enzyme. In this present study, we have focused on the complicated and hybrid systems of enzymes and metal complexes, which are quite different from the single-component system of metal complexes. We have obtained simple and reliable data of steric (crystal) structures and the corresponding electronic (optical, magnetic or electrochemical) properties and interpreted them with the conventional computational methods using the conceptual density functional theory (CDFT) framework. We have also applied some unique computational methods like molecular docking to observe the interaction pattern of laccase and a known cyanide-bridged trinuclear Ag-Cu-Ag complex. Electronic structures of the molecules and the prediction of folding of laccase enzyme were explained by the Fukui function which is supported by laccase-Ag-Cu-Ag complex docking. In this study, we have applied several computational to explore the laccase-metal complex hybrid system. Our findings can be applied in designing new compounds which can be used in growing biofuel and bioremediation industries.