Identification of IS elements in Acidithiobacillus ferrooxidans strains grown in a medium with ferrous iron or adapted to elemental sulfur

2005 ◽  
Vol 183 (6) ◽  
pp. 401-410 ◽  
Author(s):  
Tamara F. Kondrat’eva ◽  
Vasily N. Danilevich ◽  
Svetlana N. Ageeva ◽  
Grigory I. Karavaiko
2015 ◽  
Vol 1130 ◽  
pp. 97-100 ◽  
Author(s):  
Jiri Kucera ◽  
Eva Pakostova ◽  
Oldrich Janiczek ◽  
Martin Mandl

Ferric iron may act as a thermodynamically favourable electron acceptor during elemental sulfur oxidation byAcidithiobacillus ferrooxidansin extremely acidic anoxic environments. A loss of anaerobic ferric iron reduction ability has been observed in ferrous iron-grownA. ferrooxidansCCM 4253 after aerobic passaging on elemental sulfur. In this study, iron-oxidising cells aerobically adapted from ferrous iron to elemental sulfur were still able to anaerobically reduce ferric iron, however, following aerobic passage on elemental sulfur it could not. Preliminary quantitative proteomic analysis of whole cell lysates of the passage that lost anaerobic ferric iron-reducing activity resulted in 150 repressed protein spots in comparison with the antecedent culture, which retained the activity. Identification of selected protein spots by tandem mass spectrometry revealed physiologically important proteins including rusticyanin and outer-membrane cytochrome Cyc2, which are involved in iron oxidation. Other proteins were associated with sulfur metabolism such as sulfide-quinone reductase and proteins encoded by the thiosulfate dehydrogenase and heterodisulfide reductase complex operons. Furthermore, proteomic analysis identified proteins directly related to anaerobiosis. The results indicate the importance of iron-oxidising system components for anaerobic sulfur oxidation in the studied microbial strain.


2011 ◽  
Vol 102 (3) ◽  
pp. 3260-3267 ◽  
Author(s):  
Peng Chen ◽  
Lei Yan ◽  
Feifan Leng ◽  
Wenbing Nan ◽  
Xiaoxuan Yue ◽  
...  

2005 ◽  
Vol 11 (2) ◽  
pp. 59-62 ◽  
Author(s):  
Dragisa Savic ◽  
Miodrag Lazic ◽  
Vlada Veljkovic ◽  
Miroslav Vrvic

The batch oxidation kinetics of ferrous iron by Acidithiobacillus ferrooxidans were examined at different oxygen transfer rates and pH in an aerated stirred tank and a bubble column. The microbial growth, oxygen consumption rate and ferrous and ferric iron were monitored during the biooxidation. A kinetic model was established on the basis of the Michaelis-Menten kinetic equation for bacterial growth and the constants estimated from experimental data (maximum specific growth rate 0.069 h-1, saturation constant 2.9 g/dm3, and biomass yield coefficient based on ferrous iron 0.003 gd.w./gFe). Values calculated from the model agreed well with the experimental ones regardless of the bioreactor type and pH conditions.


2002 ◽  
Vol 184 (1) ◽  
pp. 313-317 ◽  
Author(s):  
Andrés Yarzábal ◽  
Gaël Brasseur ◽  
Jeanine Ratouchniak ◽  
Karen Lund ◽  
Danielle Lemesle-Meunier ◽  
...  

ABSTRACT A high-molecular-weight c-type cytochrome, Cyc2, and a putative 22-kDa c-type cytochrome were detected in the membrane fraction released during spheroplast formation from Acidithiobacillus ferrooxidans. This fraction was enriched in outer membrane components and devoid of cytoplasmic membrane markers. The genetics, as well as the subcellular localization of Cyc2 at the outer membrane level, therefore make it a prime candidate for the initial electron acceptor in the respiratory pathway between ferrous iron and oxygen.


2007 ◽  
Vol 73 (11) ◽  
pp. 3752-3754 ◽  
Author(s):  
Blanka Pokorna ◽  
Martin Mandl ◽  
Sarka Borilova ◽  
Pavla Ceskova ◽  
Romana Markova ◽  
...  

ABSTRACT Wide ranges of growth yields on sulfur (from 2.4 × 1010 to 8.1 × 1011 cells g−1) and maximum sulfur oxidation rates (from 0.068 to 1.30 mmol liter−1 h−1) of an Acidithiobacillus ferrooxidans strain (CCM 4253) were observed in 73 batch cultures. No significant correlation between the constants was observed. Changes of the Michaelis constant for sulfur (from 0.46 to 15.5 mM) in resting cells were also noted.


2009 ◽  
Vol 71-73 ◽  
pp. 745-748
Author(s):  
Tsuyoshi Sugio ◽  
Taher M. Taha ◽  
Atsunori Negishi ◽  
Fumiaki Takeuchi

Iron-grown Acidithiobacillus ferrooxidans MON-1 cells are highly resistant to organomercurial compounds as well as mercuric chloride (HgCl2). Existence of a novel Hg2+-reducing enzyme system, in which mercury resistant aa3-type cytochrome c oxidase catalyzes the reduction of Hg2+ with reduced mammalian cytochrome c or Fe2+ as an electron donor to give Hg0, has been shown in iron-grown MON-1 cells. There has been no reports on the mechanism of Hg2+ reduction by sulfur-grown A. ferrooxidans cells. The level of mercury resistance in sulfur-grown A. ferrooxidans MON-1 cells was compared with that of iron-grown MON-1 cells. Strain MON-1 was able to grow in 1% elemental sulfur medium (pH 2.5) containing 10 μM of Hg2+ or 0.2 μM phenylmercury acetate (PMA), suggesting that the levels of mercury resistance to inorganic and organic mercurial compounds are nearly the same in iron- and sulfur-grown MON-1 cells. Activity levels of Hg0 volatilization from HgCl2, PMA, and methylmercury chloride (MMC) were also nearly the same in iron- and sulfur-grown cells and these activities were markedly activated by 100 mM of Fe2+, but strongly inhibited by 1 mM of sodium cyanide, indicating that sulfur-grown MON-1 cells has the activity of ferrous iron-dependent mercury reducing enzyme system containing aa3-type cytochrome oxidase. aa3-type cytochrome c oxidase purified partially from sulfur-grown MON-1 cells showed both the iron oxidase and mercury reductase activities in the presence, but not in the absence, of rusticyanin and c-type cytochromes (Cyc1 and Cyc2) partially purified from iron-grown MON-1 cells.


2009 ◽  
Vol 160 (10) ◽  
pp. 767-774 ◽  
Author(s):  
Daniel Kupka ◽  
Maria Liljeqvist ◽  
Pauliina Nurmi ◽  
Jaakko A. Puhakka ◽  
Olli H. Tuovinen ◽  
...  

2017 ◽  
Vol 119 ◽  
pp. 59-66 ◽  
Author(s):  
Liyuan Ma ◽  
Xingjie Wang ◽  
Jiemeng Tao ◽  
Xue Feng ◽  
Xueduan Liu ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document