Immobilization of laccase on a graphene interface: Direct electron transfer and molecular dynamics study

Insights into the conformation changes of SARS-CoV-2 spike receptor-binding domain on graphene

“…All simulations were exceuted with Gromacs package 5.1.4 [40] , [41] . The interaction between RBD and graphene was simulated by CHARMM36, which is widely used to describe the molecular dynamics behavior of proteins [42] , [43] , [44] , [45] , [46] .…”

Use of Protein Engineering to Elucidate Electron Transfer Pathways between Proteins and Electrodes

“…Point mutations on the axial ligand of T1Cu site of laccase from Trametes versicolor were investigated using MD for enhanced DET abilities. 23 At first, DET properties of the native enzyme on CNTs and graphene was estimated. The laccase−electrode interface was imaged using scanning electron microscopy (SEM) to visualize the enzyme adsorbed on the graphene and CNT electrodes.…”

“…22 The π−π stacking interactions by noncovalent interactions between two aromatic surfaces are also broadly used for immobilization. 23 An additional way of enzyme immobilization is electroactive wiring, where a redoxactive polymer, such as an osmium polymer, can be deposited on an electrode and used to entrap the enzyme of interest. 24 In many cases, protein engineering for DET can help decipher internal ET mechanisms and ET to the electrode of an enzyme of interest.…”

“…Another immobilization approach is through a coordinative attachment like in the case of metal ions binding to a polyhistidine tag . The π–π stacking interactions by noncovalent interactions between two aromatic surfaces are also broadly used for immobilization . An additional way of enzyme immobilization is electroactive wiring, where a redox-active polymer, such as an osmium polymer, can be deposited on an electrode and used to entrap the enzyme of interest …”

Control of carbon monoxide dehydrogenase orientation by site-specific immobilization enables direct electrical contact between enzyme cofactor and solid surface

“…Among the various factors contributing to the efficiency of DET at the enzyme–electrode interface, it should be considered that the ET distance must be within ~14 Å 1 , 11 – 14 , since beyond this distance, the rate of ET rapidly approaches zero, as explained by the Marcus theory 6 , 15 . In addition, the enzyme should retain its bio-functionality when immobilized on the electrode surface 16 , 17 , and the formation of a stable electrode-immobilized enzyme is necessary 18 . Importantly, the enzyme on the electrode surface should adopt a so-called “electroactive” configuration, i.e., it should be within the distance that permits DET between the enzyme and the surface 11 , 19 , 20 and it should have an orientation that facilitates substrate accessibility 21 .…”