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

• DOI: 10.1073/pnas.2008741117
• Publication Date: 2020-12-07T21:49:29Z
• Authors: Yuval Agam; Ramesh Nandi; Alexander Kaushansky; Uri Peskin; Nadav Amdursky
• Keywords: Electron Transport; Porphyrins; Metals; Nanowires; Iron; Electric Impedance; Protoporphyrins; Serum Albumin, Bovine; Heme; 01 natural sciences; 0104 chemical sciences

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