The porphyrin ring rather than the metal ion dictates long-range electron transport across proteins suggesting coherence-assisted mechanism

The fundamental biological process of electron transfer (ET) takes place across proteins with common ET pathways of several nanometers. Recent discoveries push this limit and show long-range extracellular ET over several micrometers. Here, we aim in deciphering how protein-bound intramolecular cofactors can facilitate such long-range ET. In contrast to natural systems, our protein-based platform enables us to modulate important factors associated with ET in a facile manner, such as the type of the cofactor and its quantity within the protein. We choose here the biologically relevant protoporphyrin molecule as the electron mediator. Unlike natural systems having only Fe-containing protoporphyrins, i.e., heme, as electron mediators, we use here porphyrins with different metal centers, or lacking a metal center. We show that the metal redox center has no role in ET and that ET is mediated solely by the conjugated backbone of the molecule. We further discuss several ET mechanisms, accounting to our observations with possible contribution of coherent processes. Our findings contribute to our understanding of the participation of heme molecules in long-range biological ET.

Phenoxazine as a high-voltage p-type redox center for organic battery cathode materials: small structural reorganization for faster charging and narrow operating voltage

Negligible structural reorganization of phenoxazine leads to superior rate capability and a narrow voltage plateau of a lithium–organic battery.