Oxidation of elemental sulfur and sulfur compounds and CO2 fixation by Ferrobacillus ferrooxidans (Thiobacillus ferrooxidans)

1970 ◽  
Vol 16 (9) ◽  
pp. 845-849 ◽  
Author(s):  
Marvin Silver
Keyword(s):  
Co2 Fixation ◽  
Elemental Sulfur ◽  
Thiobacillus Ferrooxidans ◽  
Sulfur Compounds

The characteristics of growth of Ferrobacillus ferrooxidans on elemental sulfur are reported. This organism is not able to oxidize thiocyanate, but can oxidize elemental sulfur, sulfite, dithionite, thiosulfate, tetrathionate, and sulfide. Sulfide is only partially oxidized. All compounds that can be oxidized support CO2 fixation.

scholarly journals The production and utilization of intermediary elemental sulfur during the oxidation of reduced sulfur compounds by Thiobacillus ferrooxidans

1988 ◽  
Vol 150 (6) ◽  
pp. 574-579 ◽  
Author(s):  
W. Hazeu ◽  
W. H. Batenburg-van der Vegte ◽  
P. Bos ◽  
R. K. van der Pas ◽  
J. G. Kuenen
Keyword(s):  
Elemental Sulfur ◽  
Thiobacillus Ferrooxidans ◽  
Sulfur Compounds ◽  
Reduced Sulfur Compounds ◽  
Reduced Sulfur

OXIDATION OF INORGANIC SULFUR COMPOUNDS BY WASHED CELL SUSPENSIONS OF THIOBACILLUS FERROOXIDANS

1966 ◽  
Vol 12 (5) ◽  
pp. 957-964 ◽  
Author(s):  
J. Landesman ◽  
D. W. Duncan ◽  
C. C. Walden
Keyword(s):  
Organic Compounds ◽  
Elemental Sulfur ◽  
Thiobacillus Ferrooxidans ◽  
Sulfur Oxidation ◽  
Sulfur Compounds ◽  
Maximum Temperature ◽  
Washed Cell ◽  
Inorganic Sulfur ◽  
Respiration Rates ◽  
Growth Adaptation

Oxidation of various inorganic sulfur compounds by Thiobacillus ferrooxidans was studied, and conditions necessary for maximum respiration rates were established. Optimum oxidation of elemental sulfur occurred at pH 5.0 and gave a Qo2(N) of 726; oxidation of thiosulfate gave a maximum Qo2(N) of 514 at pH 4.0; tetra- and tri-thionate, when oxidized at pH 6.0, gave a maximum Qo2(N) of 103 and 113, respectively. Polythionates accumulated during thiosulfate oxidation, but did not during oxidation of elemental sulfur. Metallic sulfide minerals were oxidized optimally as follows: chalcopyrite, pH 2.0, maximum Qo2(N) 3200; bornite, pH 3.0, maximum Qo2(N) 450; pyrite, pH 2.0, maximum Qo2(N) 1600. Maximum temperature for oxidation of all inorganic sulfur compounds tested was 40 C.The effect of a variety of organic compounds on sulfur oxidation is presented.T. ferrooxidans requires growth adaptation on iron for maximum respiration on that substrate; however, sulfur oxidation is not inducible. Iron and sulfur can be oxidized simultaneously, giving a rate equal to the sum of the maximum rates of oxidation of the two substrates individually.

Scanning Electron Microscope Study of Bacteria on Mineral Surfaces

1976 ◽  
Vol 34 ◽  
pp. 130-131
Author(s):  
V.K. Berry
Keyword(s):  
Oxidation Reaction ◽  
Electron Microscope Study ◽  
Elemental Sulfur ◽  
Thiobacillus Ferrooxidans ◽  
Physical Contact ◽  
Metal Sulfides ◽  
Low Grade ◽  
Mineral Surfaces ◽  
Mineral Surface ◽  
Scanning Electron Microscope Study

There are two strains of bacteria viz. Thiobacillus thiooxidansand Thiobacillus ferrooxidanswidely mentioned to play an important role in the leaching process of low-grade ores. Another strain used in this study is a thermophile and is designated Caldariella .These microorganisms are acidophilic chemosynthetic aerobic autotrophs and are capable of oxidizing many metal sulfides and elemental sulfur to sulfates and Fe2+ to Fe3+. The necessity of physical contact or attachment by bacteria to mineral surfaces during oxidation reaction has not been fairly established so far. Temple and Koehler reported that during oxidation of marcasite T. thiooxidanswere found concentrated on mineral surface. Schaeffer, et al. demonstrated that physical contact or attachment is essential for oxidation of sulfur.

Sulfur-oxidizing enzyme of Ferrobacillus ferrooxidans (Thiobacillus ferrooxidans)

1968 ◽  
Vol 46 (5) ◽  
pp. 457-461 ◽  
Author(s):  
Marvin Silver ◽  
D. G. Lundgren
Keyword(s):  
Enzyme Preparation ◽  
Elemental Sulfur ◽  
Thiobacillus Ferrooxidans ◽  
Reduced Glutathione ◽  
Heme Iron ◽  
Ph Optimum ◽  
Non Heme Iron ◽  
Sulfur Oxidizing

The sulfur-oxidizing enzyme was purified about 15-fold from sulfur-grown Ferrobacillus ferrooxidans. The enzyme has a pH optimum of 7.8 and requires both elemental sulfur and reduced glutathione (GSH); however, a glutathione–polysulfide complex could also serve as substrate. The Km for GSH was determined to be 2 × 10−3 M. Non-heme iron and labile sulfide were present in the enzyme preparation, and sulfite was found to be the end product of the reaction.

scholarly journals Anaerobic Respiration of Elemental Sulfur and Thiosulfate by Shewanella oneidensis MR-1 Requires psrA, a Homolog of the phsA Gene of Salmonella enterica Serovar Typhimurium LT2

2009 ◽  
Vol 75 (16) ◽  
pp. 5209-5217 ◽  
Author(s):  
Justin L. Burns ◽  
Thomas J. DiChristina
Keyword(s):  
Gene Cluster ◽  
Salmonella Enterica ◽  
Elemental Sulfur ◽  
Shewanella Oneidensis ◽  
Anaerobic Respiration ◽  
Sulfur Cycle ◽  
Sulfur Compounds ◽  
Electron Acceptors ◽  
Inorganic Sulfur ◽  
Serovar Typhimurium

ABSTRACT Shewanella oneidensis MR-1, a facultatively anaerobic gammaproteobacterium, respires a variety of anaerobic terminal electron acceptors, including the inorganic sulfur compounds sulfite (SO3 2−), thiosulfate (S2O3 2−), tetrathionate (S4O6 2−), and elemental sulfur (S0). The molecular mechanism of anaerobic respiration of inorganic sulfur compounds by S. oneidensis, however, is poorly understood. In the present study, we identified a three-gene cluster in the S. oneidensis genome whose translated products displayed 59 to 73% amino acid similarity to the products of phsABC, a gene cluster required for S0 and S2O3 2− respiration by Salmonella enterica serovar Typhimurium LT2. Homologs of phsA (annotated as psrA) were identified in the genomes of Shewanella strains that reduce S0 and S2O3 2− yet were missing from the genomes of Shewanella strains unable to reduce these electron acceptors. A new suicide vector was constructed and used to generate a markerless, in-frame deletion of psrA, the gene encoding the putative thiosulfate reductase. The psrA deletion mutant (PSRA1) retained expression of downstream genes psrB and psrC but was unable to respire S0 or S2O3 2− as the terminal electron acceptor. Based on these results, we postulate that PsrA functions as the main subunit of the S. oneidensis S2O3 2− terminal reductase whose end products (sulfide [HS−] or SO3 2−) participate in an intraspecies sulfur cycle that drives S0 respiration.

scholarly journals Oxidation of Ferrous Iron and Elemental Sulfur by Thiobacillus ferrooxidans

1988 ◽  
Vol 54 (7) ◽  
pp. 1694-1699 ◽  
Author(s):  
Romilio T. Espejo ◽  
Blanca Escobar ◽  
Eugenia Jedlicki ◽  
Paulina Uribe ◽  
Ricardo Badilla-Ohlbaum
Keyword(s):  
Ferrous Iron ◽  
Elemental Sulfur ◽  
Thiobacillus Ferrooxidans

Toxic and immunological differences among lipopolysaccharides from Thiobacillus ferrooxidans grown autotrophically and heterotrophically

1973 ◽  
Vol 19 (11) ◽  
pp. 1335-1339 ◽  
Author(s):  
J. R. Vestal ◽  
D. G. Lundgren ◽  
K. C. Milner
Keyword(s):  
Chemical Composition ◽  
Ferrous Iron ◽  
Elemental Sulfur ◽  
Thiobacillus Ferrooxidans ◽  
Antibody Responses ◽  
Energy Sources ◽  
Agar Gel ◽  
Similar Chemical ◽  
General Chemical ◽  
Immunogenic Properties

Lipopolysaccharides (LPS) extracted from Thiobacillus ferrooxidans grown on ferrous iron, elemental sulfur, or glucose as energy source were studied for general chemical composition, toxicity, and antigenic or immunogenic properties. LPS from iron-grown cells (Fe-LPS) and from glucose-grown cells (Glu-LPS) had similar chemical composition, but that from sulfur-grown cells (S-LPS) differed significantly, especially in content of hexosamine, 2-keto-3-deoxyoctonate, and heptose. All had weak to moderate endotoxic properties, but Fe-LPS was considerably more active than the others in the several assays performed. S-LPS was very weakly immunogenic; the other two stimulated strong antibody responses in rabbits. Immunodiffusion tests in agar gel revealed marked differences among the LPS antigens of cells grown with different energy sources.

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