Results 31 to 40 of about 1,601 (181)

Electron Transfer Pathways in a Multiheme Cytochrome MtrF [PDF]

Seibutsu Butsuri, 2017
Significance Cellular respiration process in dissimilatory metal-reducing bacteria is coupled to electron transfer. In Shewanella species, a decaheme cytochrome MtrF transfers electrons to extracellular insoluble substrates, such as Fe(III) and Mn(III/IV).
Hiroshi C. Watanabe, Yuki Yamashita, Hiroshi Ishikita   +2 more
openaire   +3 more sources

Reduction Kinetic of Water Soluble Metal Salts by Geobacter sulfurreducens: Fe2+/Hemes Stabilize and Regulate Electron Flux Rates

Frontiers in Microbiology, 2022
Geobacter sulfurreducens is a widely applied microorganism for the reduction of toxic metal salts, as an electron source for bioelectrochemical devices, and as a reagent for the synthesis of nanoparticles.
Maksym Karamash, Michael Stumpe, Jörn Dengjel, Carlos A. Salgueiro, Carlos A. Salgueiro, Bernd Giese, Katharina M. Fromm   +6 more
doaj   +1 more source

Rieske Iron-Sulfur Cluster Proteins From an Anaerobic Ammonium Oxidizer Suggest Unusual Energetics in Their Parent Rieske/Cytochrome b Complexes. [PDF]

Proteins
ABSTRACT Anaerobic ammonium‐oxidizing (anammox) bacteria employ a unique, hydrazine‐based pathway to obtain energy from nitrite and ammonium. These organisms possess distinct Rieske/cytochrome b complexes whose precise role in anammox metabolism remains unclear, but which have been proposed to include the generation of NAD(P)H.
Hauser D, Sode M, Andreeva EA, Parey K, Barends TRM.   +4 more
europepmc   +2 more sources

Impact of Native Environment in Multiheme-Cytochrome Chains of the MtrCAB Complex. [PDF]

J Chem Inf Model
MtrCAB protein complex plays a crucial role in exporting electrons through the outer membrane (OM) to external acceptors. This complex consists of three proteins and contains 20 hemes. Optimal protein-protein interactions and, consequently, heme-heme interactions facilitate efficient electron transfer through the conduit of hemes.
Mandal SC, Sarangi R, Acharya A.
europepmc   +3 more sources

The Proposed Molecular Mechanisms Used by Archaea for Fe(III) Reduction and Fe(II) Oxidation

Frontiers in Microbiology, 2021
Iron (Fe) is the fourth most abundant element in the Earth’s crust where ferrous Fe [Fe(II)] and ferric Fe [Fe(III)] can be used by archaea for energy conservation.
Yiran Dong, Yiran Dong, Yawei Shan, Kemin Xia, Liang Shi, Liang Shi   +5 more
doaj   +1 more source

Redox linked flavin sites in extracellular decaheme proteins involved in microbe-mineral electron transfer [PDF]

, 2015
Extracellular microbe-mineral electron transfer is a major driving force for the oxidation of organic carbon in many subsurface environments. Extracellular multi-heme cytochromes of the Shewenella genus play a major role in this process but the mechanism
A Okamoto, AC Mitchell, AGW Leslie, AM Waterhouse, AS Beliaev, CL Reardon, D Coursolle, D Ghosal, DE Ross, DJ Richardson, DJ Richardson, DJ Richardson, DK Thompson, E Marsili, ED Brutinel, F Sievers, GF White, GM Boratyn, GN Murshudov, I Letunic, JK Fredrickson, L Shi, L Shi, MJ Daly, MJ Daly, MJ Edwards, MJ Edwards, MJ Edwards, MY El-Naggar, P Taylor, PD Adams, RJ Morris, RS Hartshorne, S Bailey, S Pirbadian, TA Clarke   +35 more
core   +1 more source

Rational engineering of Geobacter sulfurreducens electron transfer components: a foundation for building improved Geobacter-based bioelectrochemical technologies

Frontiers in Microbiology, 2015
Multiheme cytochromes have been implicated in Geobacter sulfurreducens (Gs) extracellular electron transfer (EET). These proteins are potential targets to improve EET and enhance bioremediation and electrical current production by Gs.
Joana M Dantas, Leonor eMorgado, Muktak eAklujkar, Marta eBruix, Yuri Y Londer, Marianne eSchiffer, P. Raj ePokkuluri, Carlos eSalgueiro   +7 more
doaj   +1 more source

Investigation of the Molecular Mechanisms of the Eukaryotic Cytochrome-c Maturation System

Biomolecules, 2022
Cytochromes-c are ubiquitous heme proteins with enormous impact at the cellular level, being key players in metabolic processes such as electron transfer chains and apoptosis.
Ana V. Silva, Maria O. Firmino, Nazua L. Costa, Ricardo O. Louro, Catarina M. Paquete   +4 more
doaj   +1 more source

Characterization of Shewanella oneidensis MtrC: a cell-surface decaheme cytochrome involved in respiratory electron transport to extracellular electron acceptors [PDF]

, 2007
MtrC is a decaheme c-type cytochrome associated with the outer cell membrane of Fe(III)-respiring species of the Shewanella genus. It is proposed to play a role in anaerobic respiration by mediating electron transfer to extracellular mineral oxides that ...
AI Tsapin, AJ Bard, AS Beliaev, AS Beliaev, BH Kim, Brian N. Jepson, C Myers, C Myers, C Schwalb, CR Myers, CR Myers, CR Myers, CR Myers, D Leys, David J. Richardson, DJ Richardson, E Berry, EHJ Gordon, FA Walker, GR Moore, HJ Kim, I Gautier-Luneau, J Hirst, JF Heidelberg, Jim Fredrickson, JK Fredrickson, JM Myers, JM Myers, JM Philo, John Zachara, Julea N. Butt, K Venkateswaren, KE Pitts, KH Nealson, KH Nealson, Kurnikov, L Shi, L Shi, Liang Shi, LJ Anderson, MG Almeida, MP Hendrich, MP Hendrich, PL Dutton, PS Dobbin, R Aasa, Robert S. Hartshorne, Sarah J. Field, SJ Field, T Horan, TA Clarke, Tom A. Clarke, VA Bamford   +52 more
core   +1 more source

Tethered heme domains in a triheme cytochrome allow for increased electron transport distances. [PDF]

Protein Sci
Abstract Decades of research describe myriad redox enzymes that contain cofactors arranged in tightly packed chains facilitating rapid and controlled intra‐protein electron transfer. Many such enzymes participate in extracellular electron transfer (EET), a process which allows microorganisms to conserve energy in anoxic environments by exploiting ...
Nash BW, Fernandes TM, Burton JAJ, Morgado L, van Wonderen JH, Svistunenko DA, Edwards MJ, Salgueiro CA, Butt JN, Clarke TA.   +9 more
europepmc   +2 more sources