Thiosulfate oxidation in sulfur‐reducing Shewanella oneidensis and its unexpected influences on the cytochrome c content

Author(s):  
Qingzi Yu ◽  
Weining Sun ◽  
Haichun Gao
FEBS Letters ◽  
2002 ◽  
Vol 532 (3) ◽  
pp. 333-337 ◽  
Author(s):  
Erisa Harada ◽  
Jiro Kumagai ◽  
Kiyoshi Ozawa ◽  
Shinichiro Imabayashi ◽  
Alexandre S Tsapin ◽  
...  

2012 ◽  
Vol 17 (4) ◽  
pp. 647-662 ◽  
Author(s):  
Matthew Youngblut ◽  
Evan T. Judd ◽  
Vukica Srajer ◽  
Bilal Sayyed ◽  
Tyler Goelzer ◽  
...  

Biochemistry ◽  
2014 ◽  
Vol 53 (13) ◽  
pp. 2136-2144 ◽  
Author(s):  
Matthew Youngblut ◽  
Daniel J. Pauly ◽  
Natalia Stein ◽  
Daniel Walters ◽  
John A. Conrad ◽  
...  

2012 ◽  
Vol 58 (2) ◽  
pp. 124-131 ◽  
Author(s):  
Nancy N. Perreault ◽  
Fiona H. Crocker ◽  
Karl J. Indest ◽  
Jalal Hawari

2005 ◽  
Vol 71 (8) ◽  
pp. 4935-4937 ◽  
Author(s):  
R. Bouhenni ◽  
A. Gehrke ◽  
D. Saffarini

ABSTRACT A modified mariner transposon, miniHimar RB1, was generated to mutagenize cells of the metal-reducing bacterium Shewanella oneidensis. The use of this transposon led to the isolation of stable mutants and allowed rapid identification of disrupted genes. Fifty-eight mutants, including BG104 and BG148 with transposon insertions in the cytochrome c maturation genes ccmC and ccmF1, respectively, were analyzed. Both mutants were deficient in anaerobic respiration and cytochrome c production.


1970 ◽  
Vol 48 (3) ◽  
pp. 355-363 ◽  
Author(s):  
Ronald M. Lyric ◽  
Isamu Suzuki

Thiosulfate-oxidizing enzyme was purified from Thiobacillus thioparus extracts 120- to 160-fold and the properties were studied. The enzyme had a molecular weight of 115 000 and contained 2 moles of non-heme iron. Ferricyanide was a much better electron acceptor than cytochrome c, but with cytochrome c the Km for thiosulfate was lowered from 0.1 mM to 5 μM and the pH response of the enzyme changed. Sulfite was a very strong inhibitor destroying 50% of the activity at 5 μM. The inhibition was time-dependent and essentially irreversible. Properties of the T. thioparus enzyme were compared to those of thiosulfate-oxidizing enzyme isolated from Thiobacillus neapolitanus and Ferrobacillus ferrooxidans. A pathway of thiosulfate oxidation is proposed, and metabolic roles of various enzymes studied in T. thioparus are discussed.


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