Nickel-Dithiolene Cofactors as Electron Donors and Acceptors in Protein Hosts

Metal dithiolene compounds are attracting considerable attention in the field of molecular electronics, particularly as constituents of materials with high charge-carrier mobilities. Recent experiments on cable bacteria that perform centimeter-scale charge transport suggest that Ni-bis(dithiolene) cofactors are important components of the bacterial conductive network. Further, current−voltage experiments of cable-bacteria-conductive sheaths have measured high conductivity values as compared to other electron-transfer bacteria. An important question is how the Ni-bis(dithiolene) structures participating as electron donors/acceptors contribute to the high conductivity. Currently, the protein and cofactor structures of these bacterial networks are largely unknown. Given this limitation, in this work, we explore the more general question of how Nibis(dithiolene) molecules would perform as electron donor and acceptor centers in protein-mediated charge transfer. Our aim is to deduce order-of-magnitude higher bounds for charge-transfer rates in such systems as a function of donor−acceptor distance, protein-bridge (amino acid) sequence, cofactor size, and redox state. These bounds are useful for predicting charge-transfer mechanisms and estimating rates in the absence of detailed structural information on protein wires that may use Ni-bis(dithiolene) redox cofactors. Our analysis is also relevant to the design of artificial Ni-bis(dithiolene) protein wires.