scholarly journals Reductive formation of palladium nanoparticles by Shewanella oneidensis: role of outer membrane cytochromes and hydrogenases

RSC Advances ◽  
2013 ◽  
Vol 3 (44) ◽  
pp. 22498 ◽  
Author(s):  
Chun Kiat Ng ◽  
Tian Kou Cai Tan ◽  
Hao Song ◽  
Bin Cao
Keyword(s):  
Outer Membrane ◽  
Palladium Nanoparticles ◽  
Shewanella Oneidensis

A ROLE OF PROTEINS OF THE OUTER MEMBRANE OF Shewanella oneidensis MR-1 BACTERIA IN FORMATION AND STABILIZATION OF SILVER SULFIDE NANOPARTICLES

2015 ◽  
pp. 41-48 ◽  
Author(s):  
T. A. Voeikova ◽  
A. S. Shebanova ◽  
Yu. D. Ivanov ◽  
A. L. Kaysheva ◽  
L. M. Novikova ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Shewanella Oneidensis ◽  
Silver Sulfide ◽  
Silver Sulfide Nanoparticles

scholarly journals Surface-induced formation and redox-dependent staining of outer membrane extensions inShewanella oneidensisMR-1

2019 ◽  
Author(s):  
Grace W. Chong ◽  
Sahand Pirbadian ◽  
Mohamed Y. El-Naggar
Keyword(s):  
Outer Membrane ◽  
Shewanella Oneidensis ◽  
Medium Composition ◽  
Extracellular Electron Transfer ◽  
Active Components ◽  
Transmission Electron ◽  
Redox Active ◽  
Redox Centers

AbstractThe metal-reducing bacteriumShewanella oneidensisMR-1 produces extensions of its outer membrane (OM) and periplasm that contain cytochromes responsible for extracellular electron transfer (EET) to external redox-active surfaces, including minerals and electrodes. While the role of multi-heme cytochromes in transporting electrons across the cell wall is well established, their distribution alongS. oneidensisOM extensions is also thought to allow lateral electron transport along these filaments. These proposed bacterial nanowires, which can be several times the cell length, would thereby extend EET to more distant electron acceptors. However, it is still unclear why these extensions form, and to what extent they contribute to respiration in living cells. Here, we investigate physical contributors to their formation usingin vivofluorescence microscopy. While previous studies focused on the display ofS. oneidensisouter membrane extensions (OMEs) as a response to oxygen limitation, we find that cell-to-surface contact is sufficient to trigger the production of OMEs, including some that reach >100 µm in length, irrespective of medium composition, agitation, or aeration. To visualize the extent of heme redox centers along OMEs, and help distinguish these structures from other extracellular filaments, we also performed histochemical redox-dependent staining with transmission electron microscopy on wild type and cytochrome-deficient strains. We demonstrate that redox-active components are limited to OMEs and not present on other extracellular appendages, such as pili and flagella. We also observed that the loss of 8 functional periplasmic and outer membrane cytochromes significantly decreased both the frequency and intensity of redox-dependent staining found widespread on OMEs. These results will improve our understanding of the environmental conditions that influence the formation ofS. oneidensisOMEs, as well as the distribution and functionality of EET components along extracellular appendages.

The role of proteins of the outer membrane of Shewanella oneidensis MR-1 in the formation and stabilization of silver sulfide nanoparticles

2016 ◽  
Vol 52 (8) ◽  
pp. 769-775 ◽  
Author(s):  
T. A. Voeikova ◽  
A. S. Shebanova ◽  
Yu. D. Ivanov ◽  
A. L. Kaysheva ◽  
L. M. Novikova ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Shewanella Oneidensis ◽  
Silver Sulfide ◽  
Silver Sulfide Nanoparticles

scholarly journals Role of outer membrane c-type cytochromes MtrC and OmcA in Shewanella oneidensis MR-1 cell production, accumulation, and detachment during respiration on hematite

Geobiology ◽  
2012 ◽  
Vol 10 (4) ◽  
pp. 355-370 ◽  
Author(s):  
A. C. MITCHELL ◽  
L. PETERSON ◽  
C. L. REARDON ◽  
S. B. REED ◽  
D. E. CULLEY ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Shewanella Oneidensis ◽  
Cell Production

scholarly journals Role of outer-membrane cytochromes MtrC and OmcA in the biomineralization of ferrihydrite by Shewanella oneidensis MR-1

Geobiology ◽  
2010 ◽  
Vol 8 (1) ◽  
pp. 56-68 ◽  
Author(s):  
C. L. REARDON ◽  
A. C. DOHNALKOVA ◽  
P. NACHIMUTHU ◽  
D. W. KENNEDY ◽  
D. A. SAFFARINI ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Shewanella Oneidensis

scholarly journals MexAB-OprM Efflux Pump Interaction with the Peptidoglycan of Escherichia coli and Pseudomonas aeruginosa

2021 ◽  
Vol 22 (10) ◽  
pp. 5328
Author(s):  
Miao Ma ◽  
Margaux Lustig ◽  
Michèle Salem ◽  
Dominique Mengin-Lecreulx ◽  
Gilles Phan ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Pseudomonas Aeruginosa ◽  
Cell Division ◽  
Membrane Proteins ◽  
Outer Membrane ◽  
Efflux Pump ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Active Efflux

One of the major families of membrane proteins found in prokaryote genome corresponds to the transporters. Among them, the resistance-nodulation-cell division (RND) transporters are highly studied, as being responsible for one of the most problematic mechanisms used by bacteria to resist to antibiotics, i.e., the active efflux of drugs. In Gram-negative bacteria, these proteins are inserted in the inner membrane and form a tripartite assembly with an outer membrane factor and a periplasmic linker in order to cross the two membranes to expulse molecules outside of the cell. A lot of information has been collected to understand the functional mechanism of these pumps, especially with AcrAB-TolC from Escherichia coli, but one missing piece from all the suggested models is the role of peptidoglycan in the assembly. Here, by pull-down experiments with purified peptidoglycans, we precise the MexAB-OprM interaction with the peptidoglycan from Escherichia coli and Pseudomonas aeruginosa, highlighting a role of the peptidoglycan in stabilizing the MexA-OprM complex and also differences between the two Gram-negative bacteria peptidoglycans.

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