Exemplar Abstract for Shewanella oneidensis Venkateswaran et al. 1999.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Dorothea Taylor ◽  
George M Garrity
Keyword(s):  
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

Anaerobic Respiration on Nitarsone in Aquatic Environments by Shewanella oneidensis MR-1 Lacking Known C·As lyases

2020 ◽  
Author(s):  
Dong-Feng Liu ◽  
Xue-Na Huang ◽  
Rui-Fen Cheng ◽  
Di Min ◽  
Lei Cheng ◽  
...  
Keyword(s):  
Shewanella Oneidensis ◽  
Anaerobic Respiration ◽  
Aquatic Environments

scholarly journals Expression of terminal oxidases under nutrient-limited conditions in Shewanella oneidensis MR-1

2014 ◽  
Vol 1837 ◽  
pp. e99-e100
Author(s):  
Sébastien Le Laz ◽  
Arlette Kpebe ◽  
Marielle Bauzan ◽  
Sabrina Lignon ◽  
Marc Rousset ◽  
...  
Keyword(s):  
Shewanella Oneidensis ◽  
Terminal Oxidases

Investigation of roles of divalent cations in Shewanella oneidensis pellicle formation reveals unique impacts of insoluble iron

2013 ◽  
Vol 1830 (11) ◽  
pp. 5248-5257 ◽  
Author(s):  
Jie Yuan ◽  
Yiwen Chen ◽  
Guangqi Zhou ◽  
Haijiang Chen ◽  
Haichun Gao
Keyword(s):  
Divalent Cations ◽  
Shewanella Oneidensis ◽  
Pellicle Formation

scholarly journals Identification of a Small Tetraheme Cytochromec and a Flavocytochrome c as Two of the Principal Soluble Cytochromes c inShewanella oneidensis Strain MR1

2001 ◽  
Vol 67 (7) ◽  
pp. 3236-3244 ◽  
Author(s):  
A. I. Tsapin ◽  
I. Vandenberghe ◽  
K. H. Nealson ◽  
J. H. Scott ◽  
T. E. Meyer ◽  
...  
Keyword(s):  
Binding Sites ◽  
Shewanella Oneidensis ◽  
Structural Comparison ◽  
Facultative Anaerobe ◽  
Shewanella Frigidimarina ◽  
Cytochromes C ◽  
Flavocytochrome C ◽  
Tetraheme Cytochrome ◽  
Small Tetraheme Cytochrome ◽  
Genetic Context

ABSTRACT Two abundant, low-redox-potential cytochromesc were purified from the facultative anaerobeShewanella oneidensis strain MR1 grown anaerobically with fumarate. The small cytochrome was completely sequenced, and the genes coding for both proteins were cloned and sequenced. The small cytochrome c contains 91 residues and four heme binding sites. It is most similar to the cytochromes c fromShewanella frigidimarina (formerly Shewanella putrefaciens) NCIMB400 and the unclassified bacterial strain H1R (64 and 55% identity, respectively). The amount of the small tetraheme cytochrome is regulated by anaerobiosis, but not by fumarate. The larger of the two low-potential cytochromes contains tetraheme and flavin domains and is regulated by anaerobiosis and by fumarate and thus most nearly corresponds to the flavocytochromec-fumarate reductase previously characterized fromS. frigidimarina to which it is 59% identical. However, the genetic context of the cytochrome genes is not the same for the twoShewanella species, and they are not located in multicistronic operons. The small cytochrome c and the cytochrome domain of the flavocytochrome c are also homologous, showing 34% identity. Structural comparison shows that theShewanella tetraheme cytochromes are not related to theDesulfovibrio cytochromes c 3but define a new folding motif for small multiheme cytochromesc.

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