Redox Linked Flavin Sites in Extracellular Decaheme Proteins Involved in Microbe-Mineral Electron Transfer. - Wikidata - awgldk - TriplyDB

Redox Linked Flavin Sites in Extracellular Decaheme Proteins Involved in Microbe-Mineral Electron Transfer.

Redox Linked Flavin Sites in Extracellular Decaheme Proteins Involved in Microbe-Mineral Electron Transfer.

http://www.wikidata.org/entity/Q35803147

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In Situ Analysis of a Silver Nanoparticle-Precipitating Shewanella Biofilm by Surface Enhanced Confocal Raman Microscopy Cation-limited kinetic model for microbial extracellular electron transport via an outer membrane cytochrome C complex Photoreduction of Shewanella oneidensis Extracellular Cytochromes by Organic Chromophores and Dye-Sensitized TiO2 Flavin Binding to the Deca-heme Cytochrome MtrC: Insights from Computational Molecular Simulation.Photosynthetic Microbial Fuel Cells.Electromicrobiology: realities, grand challenges, goals and predictions.Extracellular electron transfer mechanisms between microorganisms and minerals.The role of riboflavin in decolourisation of Congo red and bioelectricity production using Shewanella oneidensis-MR1 under MFC and non-MFC conditions.Exploring Step-by-Step Assembly of Nanoparticle:Cytochrome Biohybrid Photoanodes.Proton Transport in the Outer-Membrane Flavocytochrome Complex Limits the Rate of Extracellular Electron Transport.Electron transfer pathways in a multiheme cytochrome MtrF.High Performance Reduction of H2O2 with an Electron Transport Decaheme Cytochrome on a Porous ITO Electrode.Effect of oxygen on the per-cell extracellular electron transfer rate of Shewanella oneidensis MR-1 explored in bioelectrochemical systems.The Functional Mechanisms and Application of Electron Shuttles in Extracellular Electron Transfer.Extracellular Electron Transfer and Biosensors.Outer membrane cytochromes/flavin interactions in Shewanella spp.-A molecular perspective.Reply to Breuer et al.: Molecular dynamics simulations do not provide functionally relevant values of redox potential in MtrF.Bucking the current trend in bioelectrochemical systems: a case for bioelectroanalytics.Tracking Electron Uptake from a Cathode into Shewanella Cells: Implications for Energy Acquisition from Solid-Substrate Electron Donors.Structural modeling of an outer membrane electron conduit from a metal-reducing bacterium suggests electron transfer via periplasmic redox partners.Ultrastructure of Shewanella oneidensis MR-1 nanowires revealed by electron cryotomography.NanoSIMS imaging of extracellular electron transport processes during microbial iron(III) reduction

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Redox Linked Flavin Sites in Extracellular Decaheme Proteins Involved in Microbe-Mineral Electron Transfer.

http://www.wikidata.org/entity/Q35803147

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2015 nî lūn-bûn

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2015年論文

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2015年论文

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Redox Linked Flavin Sites in E ...... obe-Mineral Electron Transfer.

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Redox Linked Flavin Sites in E ...... obe-Mineral Electron Transfer.

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Redox Linked Flavin Sites in E ...... obe-Mineral Electron Transfer.

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Redox Linked Flavin Sites in E ...... obe-Mineral Electron Transfer.

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Redox Linked Flavin Sites in E ...... obe-Mineral Electron Transfer.

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Redox Linked Flavin Sites in E ...... obe-Mineral Electron Transfer.

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Scientific Reports

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Redox Linked Flavin Sites in E ...... obe-Mineral Electron Transfer.

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Alice Tome-Fernandez

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David J Richardson

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Gaye F White

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Jim K Fredrickson

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John M Zachara

http://www.w3.org/2001/XMLSchema#string

Liang Shi

http://www.w3.org/2001/XMLSchema#string

Marcus J Edwards

http://www.w3.org/2001/XMLSchema#string

Michael Norman

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P2860

Protein oxidation implicated as the primary determinant of bacterial radioresistance

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Jalview Version 2--a multiple sequence alignment editor and analysis workbench

Structural and mechanistic mapping of a unique fumarate reductase

Structure of a bacterial cell surface decaheme electron conduit

The crystal structure of the extracellular 11-heme cytochrome UndA reveals a conserved 10-heme motif and defined binding site for soluble iron chelates

Integration of macromolecular diffraction data

Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega

REFMAC5 for the refinement of macromolecular crystal structures

The CCP4 suite: programs for protein crystallography

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10.1038/SREP11677

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5

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Emma V Ainsworth

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2015-07-01T00:00:00Z

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