Bacterial pyrite oxidation I. The effect of pure and mixed cultures of Thiobacillus ferrooxidans and Thiobacillus thiooxidans on release of iron.

Wakao, Norio; Mishina, Masatoshi; Sakurai, Yonekichi; Shiota, Hideo

doi:10.2323/jgam.28.331

Cited by 32 publications

(11 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Comparative studies of amino acid sequences have revealed that, although the large subunit is highly conserved, the small subunit has undergone significant divergence. In addition to such comparative analyses, site-directed mutagenesis and chemical modification methods have identified the functional ferrooxidans Fel cells, kindly provided by H. Shiota (Iwate University, Japan), were grown in inorganic 9K medium (51) and used as a source of chromosomal DNA and total RNA (59). The multicopy plasmids pUC18 and pUC19 were used as cloning vectors (40).…”

mentioning

confidence: 99%

Evidence for two sets of structural genes coding for ribulose bisphosphate carboxylase in Thiobacillus ferrooxidans

et al. 1991

View full text Add to dashboard Cite

Previously, we reported the cloning of the ribulose-1,5-bisphosphate carboxylase genes (rbcLI-rbcSl) of Thiobacillusferrooxidans Fel (T. Kusano, K. Sugawara, C. Inoue, and N. Suzuki, Curr. Microbiol. 22:35-41, 1991). With these genes as probes, a second set of ribulose-1,5-bisphosphate carboxylase genes (rbcL2-rbcS2) was identified in the same strain and cloned. rbcLI and rbcL2 encode the large subunits, and rbcSI and rbcS2 encode the small subunits. Similar restriction patterns between these gene sets suggested a high level of sequence homology. In fact, sequence analysis showed that a 2.2-kb region, including the entire large and small subunit structural genes, was totally conserved in rbcLl-rbcSI and rbcL2-rbcS2. The rbcLl (rbcL2) and rbcSI (rbcS2) genes were 1,422 and 333 bp in length and encoded 473-and 110-amino-acid proteins, respectively. The genes were separated by a 90-bp spacer sequence and were preceded by possible ribosome-binding sites. The N-terminal amino acid sequences of the subunit proteins, synthesized in Escherichia coli, were determined by Edman degradation and found to agree with the deduced amino acid sequences, except for the N-terminal methionine residue. The transcriptional start site of the rbc genes was determined by primer extension, and the size of the rbc transcript was estimated to be about 2.1 kb, suggestive of the cotranscription of rbcLl-rbcSI and/or rbcL2-rbcS2 mRNAs. Comparisons of amino acid sequences of both subunits with those of other organisms revealed that the ribulose-1,5-bisphosphate carboxylase of T. ferrooxidans, a chemoautotrophic bacterium, is phylogenetically closer to the photosynthetic bacterium Chromatium vinosum than to another chemoautotrophic bacterium, Alcaligenes eutrophus. essentiality of certain amino acid residues of the RuBPCase gene products (3,17,18,42).In prokaryotes, it is known that the genes encoding the large and small subunits of RuBPCase are very closely linked and that both genes are cotranscribed (38, 48), differing from the case in higher plants.The presence of two sets of RuBPCase genes has been reported in certain organisms; for example, in R. sphaeroides (11,53,58), Alcaligenes eutrophus (2, 21, 26), Chromatium vinosum (27,56,57), and Nitrobacter hamburgensis (15). In A. eutrophus, one set is located chromosomally and the other is on the megaplasmid (2, 26).Previously, we reported the cloning of one set of the entire large and small subunit genes (rbcLl-rbcSI) of T. ferrooxidans Fel and on the expression of the genes when under the control of a tac promoter in Escherichia coli (28). We now report the cloning of a second set (rbcL2-rbcS2) of RuBP Case genes from the same strain of T. ferrooxidans, and we present the nucleotide sequence of the two sets and their deduced amino acid sequences. T. ferrooxidans RuBPCase genes are more closely related to those from a y-purple photosynthetic bacterium, C. vinosum, than to a chemolithotrophic bacterium, A. eutrophus. Evidence is also presented that the sequences over a 2.2-kb region covering t...

show abstract

mentioning

confidence: 99%

Evidence for two sets of structural genes coding for ribulose bisphosphate carboxylase in Thiobacillus ferrooxidans

et al. 1991

View full text Add to dashboard Cite

show abstract

“…A strain of T. thiooxidans 53 was kindly supplied by Dr. H. Shiota (Iwate University) (13). It was cultivated chemolithotrophically in Silverman 9K medium (10) containing 1 % sulfur powder.…”

Section: Methodsmentioning

confidence: 99%

Long-term stabilization of sulfite oxidation in whole cells of Thiobacillus thiooxidans S3.

Nakamura

Fukuda

Amano

1990

J. Gen. Appl. Microbiol.

View full text Add to dashboard Cite

We studied different factors which affect sulfite oxidation in Thiobacillus thiooxidans S3 cells during storage. The cells continued the oxidation for 27 days when they were preserved at 4°C in a 0.1 M citrate buffer (pH 6.0), or for 22 days when 20°c glycerol was added to the same buffer and storage was at -20 °C. When the cells were stored at 4°C, they kept full activity even after 45 days. If the cells were immobilized before they were stored at 4°C in the buffer, they kept their full activity for 90 days. The cells treated by lyophilization or drying at room temperature lost about 90°c of the original activity. T. thiooxidans S3 cells were more stable than T. novel/us cells under the same storage conditions. Thiobacillus thiooxidans has been studied for a long time since their discovery by Waksman and Joffe (14). Although many authors (3, 4,12) have studied this organism from various view points, the progress of those studies has been relatively slow compared to that for heterotrophs. This is because of the slower growth rate and the very low cell yield of this organism. We have usually obtained no more than 0.3 g of dry cells in 10 day cultures of 1,000 ml broth. Recently, the organism's growth in extreme conditions of temperature, pH, salinity and pressure, have been reported. T. thiooxidans can grow in extremely low pH environments, but the characters of the organism, including the enzyme system of sulfur, thiosulfate, or sulfite oxidation, were obscure until now. When we tried to study this organism, we had trouble obtaining quantities of cells having sufficient activity. So mass production culture or a cell accumulation method by storage was needed to obtain enough cells. However, it is not easy to frequently operate several hundred-liter fermentor (11). It is also difficult to preserve cells keeping high metabolite activity for a long storage period. This paper describes a preservation method which is * Address Biotechnology, reprint requests to:Faculty of Engineering

show abstract

“…Strains Fe l and Fe2 belong to T. ferrooxidans. Fe l has often been used in our studies (25)(26)(27). However, strains Fel and Fe2 are different in their ability to oxidize sulfur and thiosulfate.…”

Section: Discussionmentioning

confidence: 99%

“…We studied the ecological aspects of acidophilic chemolithotrophic iron-and sulfur-oxidizing bacteria at the abandoned Matsuo sulfur and iron sulfide (pyrite) mine areas (21,22,24) and the leaching of pyrite ores by the bacteria (25)(26)(27). We found that iron-and sulfur-oxidizing bacteria were ubiquitously distributed in both acid mine waters and pyrite ores, and were responsible for the rapid oxidation of iron and sulfur and the degradation of the ores.…”

mentioning

confidence: 99%

Morphological, physiological, and chemotaxonomical characteristics of iron- and sulfur-oxidizing bacteria isolated from acid mine drainage waters.

Wakao

Hanada

Takahashi

et al. 1991

J. Gen. Appl. Microbiol.

Self Cite

View full text Add to dashboard Cite

Two strains, Fe 1 and Fe2, of iron-oxidizing bacteria from acid drainage water at the Matsuo mine showed dissimilar characteristics of red-brown colonies on FeSO4-9K silica gel plates. The Fe l colonies were large and irregular. The Fe2 colonies were minute and circular. These bacteria, identified as Thiobacillus ferrooxidans on the basis of their physiological and chemotaxonomical properties (fatty acid composition, ubiquinone type, andl DNA base composition), were different strains. Fe2 differed from Fe l in its extremely low oxidizing activity of sulfur and thiosulfate. Two strains, S2 and S3, of sulfur-oxidizing bacteria were separately isolated on Na2SzO3-9K silica gel plates and agar plates, respectively. However, S2 and S3 formed pale brown and pale yellow colonies on the silica gel and agar plates, respectively. Since these two strains were identical in their properties, they were judged to be quite similar or the same strain. From their morphological, physiological, and chemotaxonomical properties, they were identified as Thiobacillus thiooxidans. The oxidation characteristics of both sulfur and thiosulfate by the strains of iron-and sulfur-oxidizing bacteria were also investigated.The sulfur-oxidizing bacterium Thiobacillus thiooxidans was first isolated in 1921 from soil (28). Twenty-six years later Colmer and Hinkle reported the first isolation of Thiobacillus ferrooxidans responsible for the oxidation of iron and inorganic sulfur compounds from the acid mine drainage of bituminous coal mines (1). Since then, the iron-and sulfur-oxidizing Thiobacillus species were shown to occur widely in nature especially where oxidisable sulfur and iron are

show abstract

Bacterial pyrite oxidation I. The effect of pure and mixed cultures of Thiobacillus ferrooxidans and Thiobacillus thiooxidans on release of iron.

Cited by 32 publications

References 0 publications

Evidence for two sets of structural genes coding for ribulose bisphosphate carboxylase in Thiobacillus ferrooxidans

Evidence for two sets of structural genes coding for ribulose bisphosphate carboxylase in Thiobacillus ferrooxidans

Long-term stabilization of sulfite oxidation in whole cells of Thiobacillus thiooxidans S3.

Morphological, physiological, and chemotaxonomical characteristics of iron- and sulfur-oxidizing bacteria isolated from acid mine drainage waters.

Contact Info

Product

Resources

About