Results 11 to 20 of about 885 (161)

Comparative structure-potentio-spectroscopy of the Shewanella outer membrane multiheme cytochromes [PDF]

Current Opinion in Electrochemistry, 2017
Many species of bacteria can generate energy in the anoxic subsurface by directly coupling intracellular oxidative reactions to the reduction of extracellular metal oxides. Coupling these processes requires electron transfer networks that extend from the
Butt, Julea N., Clarke, Thomas A., Edwards, Marcus J., Gates, Andrew J., Richardson, David J.   +4 more
core   +5 more sources

Photosensitised Multiheme Cytochromes as Light‐Driven Molecular Wires and Resistors [PDF]

ChemBioChem, 2018
Multiheme cytochromes possess closely packed redox‐active hemes arranged as chains spanning the tertiary structure. Here we describe five variants of a representative multiheme cytochrome engineered as biohybrid phototransducers for converting light into
Anderson, Bachmeier, Balzani, Breuer, Breuer, Cannizzo, Cedervall, Cheesman, Clarke, Czjzek, Damrauer, Edwards, Fonseca, Fruton, Gao, Geren, Geren, Gray, Guerois, Gust, Hagfeldt, Harada, Hermann, Innocenzi, Inoue, Jiang, Kato, Kokhan, Krieger, Kumar, Kumar, Kärkäs, Lam, Leys, Lovley, Manke, Mayhew, Miller, Millett, Montoya, Paquete, Paquete, Pellegrin, Peters, Prasad, Qian, Rillema, Roth, Sasaki, Schmidt, Schuergers, Schwizer, Schymkowitz, Sciuto, Shi, Shi, Soltau, Soltau, Soltau, Tezcan, Van Durme, White, Willkomm, Woolerton   +63 more
core   +6 more sources

Increased mutation rates and diversity are dominant features of Geobacter multiheme cytochromes

mBio
Multiheme cytochromes (MHCs) are the central catalysts of extracellular electron transfer and are uniquely abundant in the genomes of model Fe(III)-reducing organisms like Geobacter sulfurreducens.
Ruth Starwalt-Lee, Jeffrey A. Gralnick, Daniel R. Bond   +2 more
doaj   +2 more sources

Mimicking Natural Photosynthesis: Designing Ultrafast Photosensitized Electron Transfer into Multiheme Cytochrome Protein Nanowires [PDF]

Nanomaterials, 2020
Efficient nanomaterials for artificial photosynthesis require fast and robust unidirectional electron transfer (ET) from photosensitizers through charge-separation and accumulation units to redox-active catalytic sites.
Daniel R. Marzolf, Aidan M. McKenzie, Matthew C. O’Malley, Nina S. Ponomarenko, Coleman M. Swaim, Tyler J. Brittain, Natalie L. Simmons, Phani Raj Pokkuluri, Karen L. Mulfort, David M. Tiede, Oleksandr Kokhan   +10 more
doaj   +3 more sources

Ultrafast Light-Driven Electron Transfer in a Ru(II)tris(bipyridine)-Labelled Multiheme Cytochrome [PDF]

Journal of the American Chemical Society, 2019
Multiheme cytochromes attract much attention for their electron transport properties. These proteins conduct electrons across bacterial cell walls, along extracellular filaments, and when purified can serve as bionanoelectronic junctions.
Adamczyk, Katrin, Blumberger, Jochen, Butt, Julea N., Carof, Antoine, Clarke, Thomas A., Hall, Christopher R., Heisler, Ismael, Jiang, Xiuyun, Meech, Stephen R., Piper, Samuel E. H., Sazanovich, Igor V., Towrie, Michael, van Wonderen, Jessica H., Watmough, Nicholas J.   +13 more
core   +11 more sources

Electron transport across the cell envelope via multiheme c-type cytochromes in Geobacter sulfurreducens

Frontiers in Chemistry
Extracellular electron transfer (EET) enables certain microorganisms to respire using soluble and insoluble extracellular electron acceptors by transporting electrons across the cell envelope. Among these, G. sulfurreducens serves as a model organism for
Media Zakizadeh Tabari, Allon I. Hochbaum   +1 more
doaj   +3 more sources

Delineating redox cooperativity in water‐soluble and membrane multiheme cytochromes through protein design

Protein Science, Volume 33, Issue 8, August 2024.
Abstract Nature has evolved diverse electron transport proteins and multiprotein assemblies essential to the generation and transduction of biological energy. However, substantially modifying or adapting these proteins for user‐defined applications or to gain fundamental mechanistic insight can be hindered by their inherent complexity.
Benjamin J. Hardy, Paulina Dubiel, Ethan L. Bungay, May Rudin, Christopher Williams, Christopher J. Arthur, Matthew J. Guberman‐Pfeffer, A. Sofia Oliveira, Paul Curnow, J. L. Ross Anderson   +9 more
wiley   +4 more sources

Tunneling-to-Hopping Transition in Multiheme Cytochrome Bioelectronic Junctions

The Journal of Physical Chemistry Letters, 2023
Multiheme cytochromes (MHCs) have attracted much interest for use in nanobioelectronic junctions due to their high electronic conductances. Recent measurements on dry MHC junctions suggested that a coherent tunneling mechanism is operative over surprisingly long long distances (>3 nm), which challenges our understanding of coherent transport phenomena.
Zdenek Futera, Xiaojing Wu, Jochen Blumberger   +2 more
openaire   +3 more sources

Role of multiheme cytochromes involved in extracellular anaerobic respiration in bacteria [PDF]

Protein Science, 2019
AbstractHeme containing proteins are involved in a broad range of cellular functions, from oxygen sensing and transport to catalyzing oxidoreductive reactions. The two major types of cytochrome (b‐type and c‐type) only differ in their mechanism of heme attachment, but this has major implications for their cellular roles in both localization and ...
Edwards, Marcus J., Richardson, David J., Paquete, Catarina M., Clarke, Thomas A.   +3 more
openaire   +4 more sources

Modification of bacterial cell membrane to accelerate decolorization of textile wastewater effluent using microbial fuel cells: role of gamma radiation [PDF]

, 2020
The aim of the present work was to increase bacterial adhesion on anode via inducing membrane modifications to enhance textile wastewater treatment in Microbial Fuel Cell (MFC).
Abd El Kareem, H., Abd El Kareem, H., Bowman, K., Bowman, K., Breheny, M., Breheny, M., Fathy, R., Fathy, R., Gamal, M., Gamal, M., Gomaa, O., Gomaa, O., Keshavarz, T., Keshavarz, T., Kyazze, G., Kyazze, G., Maghrawy, H., Maghrawy, H., Selim, N., Selim, N.   +19 more
core   +1 more source