by Keyword: Electron-transport

Pankratov, Dmitrii, Martinez, Silvia Hidalgo, Karman, Cheryl, Gerzhik, Anastasia, Gomila, Gabriel, Trashin, Stanislav, Boschker, Henricus T S, Geelhoed, Jeanine S, Mayer, Dirk, De Wael, Karolien, Meysman, Filip J R, (2024). The organo-metal-like nature of long-range conduction in cable bacteria Bioelectrochemistry 157, 108675

Cable bacteria are filamentous, multicellular microorganisms that display an exceptional form of biological electron transport across centimeter-scale distances. Currents are guided through a network of nickel-containing protein fibers within the cell envelope. Still, the mechanism of long-range conduction remains unresolved. Here, we characterize the conductance of the fiber network under dry and wet, physiologically relevant, conditions. Our data reveal that the fiber conductivity is high (median value: 27 S cm-1; range: 2 to 564 S cm-1), does not show any redox signature, has a low thermal activation energy (Ea = 69 +/- 23 meV), and is not affected by humidity or the presence of ions. These features set the nickel-based conduction mechanism in cable bacteria apart from other known forms of biological electron transport. As such, conduction resembles that of an organic semi-metal with a high charge carrier density. Our observation that biochemistry can synthesize an organometal-like structure opens the way for novel bio-based electronic technologies.

JTD Keywords: 'current, Activation energy, Bacteria, Bioelectronic, Bioelectronics, Cable bacteria, Cables, Centimeter-scale, Electrochemical impedance spectroscopy, Electrochemical-impedance spectroscopies, Electron transport, Electron transport properties, Electron-transport, Long -distance electron transport, Long-distance electron transport, Microbial nanowires, Nickel, Nickel containing, Protein conductivity, Protein fibers, Proteins, Sulfur

López-Ortiz, M, Zamora, RA, Giannotti, MI, Gorostiza, P, (2023). The Protein Matrix of Plastocyanin Supports Long-Distance Charge Transport with Photosystem I and the Copper Ion Regulates Its Spatial Span and Conductance Acs Nano 17, 20334-20344

Charge exchange is the fundamental process that sustains cellular respiration and photosynthesis by shuttling electrons in a cascade of electron transfer (ET) steps between redox cofactors. While intraprotein charge exchange is well characterized in protein complexes bearing multiple redox sites, interprotein processes are less understood due to the lack of suitable experimental approaches and the dynamic nature of the interactions. Proteins constrained between electrodes are known to support electron transport (ETp) through the protein matrix even without redox cofactors, as the charges housed by the redox sites in ET are furnished by the electrodes. However, it is unknown whether protein ETp mechanisms apply to the interprotein medium present under physiological conditions. We study interprotein charge exchange between plant photosystem I (PSI) and its soluble redox partner plastocyanin (Pc) and address the role of the Pc copper center. Using electrochemical scanning tunneling spectroscopy (ECSTS) current-distance and blinking measurements, we quantify the spatial span of charge exchange between individual Pc/PSI pairs and ETp through transient Pc/PSI complexes. Pc devoid of the redox center (Pcapo) can exchange charge with PSI at longer distances than with the copper ion (Pcholo). Conductance bursts associated with Pcapo/PSI complex formation are higher than in Pcholo/PSI. Thus, copper ions are not required for long-distance Pc/PSI ETp but regulate its spatial span and conductance. Our results suggest that the redox center that carries the charge in Pc is not necessary to exchange it in interprotein ET through the aqueous solution and question the canonical view of tight complex binding between redox protein partners.

JTD Keywords: azurin, binding, blinking, crystal-structure, cupredoxin, current distance spectroscopy, electrochemical tunneling microscopy, proteinconductance, reduction, single metalloprotein, single molecule measurements, site, spectroscopy, Blinking, Cupredoxin, Current distance spectroscopy, Electrochemical tunneling microscopy, Interprotein electron transfer, Protein conductance, Single molecule measurements, State electron-transport

Diez-Perez, Ismael, Hihath, Joshua, Hines, Thomas, Wang, Zhong-Sheng, Zhou, Gang, Mullen, Klaus, Tao, Nongjian, (2011). Controlling single-molecule conductance through lateral coupling of [pi] orbitals Nature Nanotechnology , 6, (4), 226-231

In recent years, various single-molecule electronic components have been demonstrated(1). However, it remains difficult to predict accurately the conductance of a single molecule and to control the lateral coupling between the pi orbitals of the molecule and the orbitals of the electrodes attached to it. This lateral coupling is well known to cause broadening and shifting of the energy levels of the molecule; this, in turn, is expected to greatly modify the conductance of an electrodemolecule- electrode junction(2-6). Here, we demonstrate a new method, based on lateral coupling, to mechanically and reversibly control the conductance of a single-molecule junction by mechanically modulating the angle between a single pentaphenylene molecule bridged between two metal electrodes. Changing the angle of the molecule from a highly tilted state to an orientation nearly perpendicular to the electrodes changes the conductance by an order of magnitude, which is in qualitative agreement with theoretical models of molecular pi-orbital coupling to a metal electrode. The lateral coupling is also directly measured by applying a fast mechanical perturbation in the horizontal plane, thus ruling out changes in the contact geometry or molecular conformation as the source for the conductance change.

JTD Keywords: Junction conductance, Electron-transport, Interface, Dependence, Mechanism, Length