The electron transfer in cytochrome proteins has different emerging applications in biosensing and bio-energy, such as detecting nitric oxide and sensing long-wavelength infrared in bolometer. The efficiency of the electron transfer is highly dependent on the adsorbed protein’s orientations and structure, particularly the orientations and positions of the heme rings. In this work, we developed a hybrid simulation scheme of atomistic molecular dynamics (MD) simulation, free energy computation and kinetic Monte Carlo (KMC) simulation to study the electron transfer (ET) of the decaheme cytoheme (MtrF) from the metal-respiring bacteria, Shewanella oneidensis MR-1, on graphene surface. The orientations of MtrF on a graphene surface were predicted based on the binding free energy, which incorporates the important driving force of the protein and surface dehydration besides protein-surface interactions. MD simulations were performed to investigate the protein structural relaxation on a graphene surface. The effect of the adsorbed protein’s structural rearrangement on ET was further investigated by KMC simulation.

Adsorption and electron transfer of deca-heme cytochrome (MtrF) studied with atomistic simulations and kinetic Monte Carlo simulation

251st National Meeting (2016)

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