Removal of H2S by the purple sulphur bacterium Ectothiorhodospira shaposhnikovii

1994 ◽  
Vol 10 (1) ◽  
pp. 110-111 ◽  
Author(s):  
M. B. Vainshtein ◽  
G. I. Gogotova ◽  
N. -J. Heinritz



2020 ◽  
Vol 70 (11) ◽  
pp. 5701-5710 ◽  
Author(s):  
Mohit Kumar Saini ◽  
Weng ChihChe ◽  
Nathan Soulier ◽  
Aswathy Sebastian ◽  
Istvan Albert ◽  
...  

A novel thermophilic phototrophic purple sulphur bacterium was isolated from microbial mats (56 °C) at Nakabusa hot springs, Nagano prefecture, Japan. Cells were motile, rod-shaped, stain Gram-negative and stored sulphur globules intracellularly. Bacteriochlorophyll a and carotenoids of the normal spirilloxanthin series were the major pigments. Dense liquid cultures were red in colour. Strain No.7T was able to grow photoautotrophically using sulfide, thiosulfate, sulfite and hydrogen (in the presence of sulfide) as electron donors and bicarbonate as the sole carbon source. Optimum growth occurred under anaerobic conditions in the light at 50 °C (range, 40–56 °C) and pH 7.2 (range, pH 7–8). Major fatty acids were C16 : 0 (46.8 %), C16 : 1 ω7c (19.9 %), C18 : 1 ω7c (21.1 %), C14 : 0 (4.6 %) and C18 : 0 (2.4 %). The polar lipid profile showed phosphatidylglycerol and unidentified aminophospholipids to be the major lipids. The only quinone detected was ubiquinone-8. 16S rRNA gene sequence comparisons indicated that the novel bacterium is only distantly related to Thermochromatium tepidum with a nucleotide identity of 90.4 %. The phylogenetic analysis supported the high novelty of strain No.7T with a long-branching phylogenetic position within the Chromatiaceae next to Thermochromatium tepidum . The genome comprised a circular chromosome of 2.99 Mbp (2 989 870 bp), included no plasmids and had a DNA G+C content of 61.2 mol%. Polyphasic taxonomic analyses of the isolate suggested strain No.7T is a novel genus within the Chromatiaceae . The proposed genus name of the second truly thermophilic purple sulphur bacterium is Caldichromatium gen. nov. with the type species Caldichromatium japonicum sp. nov. (DSM 110881=JCM 39101).



1971 ◽  
Vol 178 (1052) ◽  
pp. 301-326 ◽  

The gas vacuoles which occur in various prokaryotic organisms can be estimated quantitatively by the change in light scattering which takes place when they are destroyed by pressure. The gradual disappearance of gas vacuoles under rising pressure is explained by the intrinsic variation in critical collapse pressure of their constituent gas vesicles. These collapse instantaneously at pressures exceeding their critical pressure, but withstand repeated and prolonged application of pressures below this value. Gas vesicle membranes are freely permeable to gases, and as a consequence the vacuole gas is at atmospheric pressure in aerated suspensions. Increasing or decreasing the pressure of gas in the gas vacuoles brings about a corresponding change in the pressure required to collapse them, indicating that the vacuole gas helps to support the structure. Pressures in excess of the vacuole gas pressure are borne by the membrane itself. The pressure required to collapse gas vacuoles present in blue-green algae is increased if the cells are suspended in a hypertonic sucrose solution, because this removes the cell turgor pressure acting on them. This observation, which confirms the classical theory on the osmotic relationships of plant cells, provides the first reliable method of estimating turgor pressures in prokaryotic organisms. Cell turgor pressure was found to be higher in a blue-green alga than in a purple sulphur bacterium investigated; no cell turgor could be detected in a halobacterium which grows in saturated brines, suggesting that the salt concentration must be the same inside and outside the cell. The gas vesicles in these organisms seemed to be adapted to withstand the pressures they were likely to encounter, those of the alga being the strongest, and those of the halobacterium the weakest. Even so, the range of turgor pressure overlapped the critical pressure range of the gas vesicles in the alga and purple sulphur bacterium so that turgor pressure alone may effect their collapse under certain circumstances. With the alga this seems to happen in conditions promoting photosynthesis, providing the organism with a means of regulating its buoyancy. It is suggested that the width of a gas vesicle is important in determining its strength, and that this explains the differences in size and shape of the gas vesicles which have evolved in the three organisms. Interfacial tension could in theory exert considerable pressures on the highly curved surface of a gas vesicle but this effect would be minimized if its outer surface were of a hydrophilic nature. Several observations have been made which support this idea. Pressures generated by centrifugation will collapse isolated gas vesicles and must be considered when using this technique to purify them. Sufficient pressure to collapse gas vesicles can also be developed in small columns by the massive negative accelerations developed in collisions. This phenomenon, which may have application in engineering fields, must also be reckoned with in handling these pressure-sensitive structures. It is concluded that even though the gas vesicle membrane must tear during its collapse, the gas it contains diffuses away rather than escaping as a bubble.



1979 ◽  
Vol 177 (3) ◽  
pp. 819-823 ◽  
Author(s):  
R P Ambler ◽  
M Daniel ◽  
T E Meyer ◽  
R G Bartsch ◽  
M D Kamen

An amino acid sequence is proposed for the cytochrome c′ from the photosynthetic purple sulphur bacterium Chromatium vinosum strain D. It is single polypeptide chain of 131 residues, with haem-attachment cysteine residues at positions 121 and 124. The results discredit an earlier report [Dus, Bartsch & Kamen (1962) J. Biol. Chem 237, 3083–3093] of a di-haem peptide sequence from this protein. The sequence belongs to the same class as the published Alcal!igenes and Rhodospirillum rubrum cytochrome c′ squences, but the resemblance is not close. Detailed evidence for the amino acid sequence of the protein has been deposited as Supplementary Publication SUP 50,093 (15 pp.) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1978) 169, 5.



1993 ◽  
Vol 160 (2) ◽  
pp. 96-100 ◽  
Author(s):  
Nikolaj A. Zorin ◽  
Peter Lindblad


2006 ◽  
Vol 62 (a1) ◽  
pp. s125-s125
Author(s):  
I. Tomcová ◽  
R. M. M. Branca ◽  
Cs. Bagyinka ◽  
G. Bodó ◽  
I. Kutá Smatanová


2014 ◽  
Vol 1837 (11) ◽  
pp. 1849-1860 ◽  
Author(s):  
Anne-Marie Carey ◽  
Kirsty Hacking ◽  
Nichola Picken ◽  
Suvi Honkanen ◽  
Sharon Kelly ◽  
...  




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