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PubMed1980

Thermothrix thiopara: Growth and Metabolism of a Newly Isolated Thermophile Capable of Oxidizing Sulfur and Sulfur Compounds.

Thermothrix thiopara is isolated from hot sulfur springs. It occurs in situ at a temperature of 72 degrees C, a pH of 7.0, and an HS concentration of 17.4 mumol/liter (0.8 ppm). The organism was capable of autotrophic growth. Sulfite, sulfur, and polythionates were formed and subsequently degraded to sulfate during growth with thiosulfate as the sole energy source. Thiosulfate was oxidized by the polythionate pathway, and the stoichiometry of growth on thiosulfate was determined. The organism was also capable of heterotrophic growth in amino acids and simple sugars. A source of reduced sulfur (methionine, glutathione) was required for heterotrophic growth. Growth occurred aerobically or anaerobically with nitrate as a terminal oxidant. Both nitrous oxide and dinitrogen were produced. At 73 degrees C the maximum autotrophic growth rate in batch culture using thiosulfate was 0.56 generation per h. Under the same conditions in continuous culture, washout occurred at a dilution rate of 0.3 to 0.4 per h, corresponding to a cellular growth rate of 0.43 to 0.58 generation per h. This was nearly three times the growth rate for Thiobacillus denitrificans. T. thiopara is gram negative. It was also found to be both lysozyme and penicillin susceptible. As a result, this organism cannot be considered an archaebacterium.

Journal Article↗
PubMed2001

[Pharmaceutical importance of Allium sativum L. 1. Organic sulfur compounds and their transformation based on present knowledge].

The paper sums up new experimental knowledge concerning the individual groups of organic sulfurous substances of the garlic: sulfoxides, thiosulfinate, ajoens, vinyldithiines, alkyl and alkene sulfides and glutamylpeptides of sulfurous amino acids, their transformation reactions (based on the temperature, pH, extraction medium, and time) and the final products of transformations (Scheme 1, 2). It deals with the activity of the enzyme alliinase necessary for the transformation of sulfoxides present in the whole garlic, its isolation and stability as well as the stability of the dominant thiosulfinate allicin in various media and simulated body fluids. It refers to the studies of the metabolism and transformations of the most important sulfurous components performed in vitro on the hepatocytes and on the isolated rat liver, and those carried out in vivo on the rats and including the examination of the composition of the exhaled air. It follows from published papers that all different degradation products of thiosulfinates, mainly the prevailing allicin, are carriers of various biological activities. The paper also lists the types of commercial preparations prepared from the garlic, their differences, and considerable variability of their contents of active principles.

Animals↗
PubMed2001

Sulfur-centered reactive intermediates derived from the oxidation of sulfur compounds of biological interest.

Sulphur compounds play a central role in the structure and activity of many vital systems. In the living cell, sulfur constitutes an essential part of the defense against oxidative damage and is transformed into a variety of sulfur free radical species. Many studies of the chemistry of sulfur-centered radicals using pulse radiolysis and photolysis techniques to detect and measure the kinetics of these radicals have been published and reviewed. This paper discusses the present state of research on the formation and reactivity of certain sulfur-centered radicals [RS*, RSS*, RS*+, (RSSR)*+] and their implications for biological systems.

Free Radicals↗
PubMed2002

An exported rhodanese-like protein is induced during growth of Acidithiobacillus ferrooxidans in metal sulfides and different sulfur compounds.

By proteomic analysis we found a 21-kDa protein (P21) from Acidithiobacillus ferrooxidans ATCC 19859 whose synthesis was greatly increased by growth of the bacteria in pyrite, thiosulfate, elemental sulfur, CuS, and ZnS and was almost completely repressed by growth in ferrous iron. After we determined the N-terminal amino acid sequence of P21, we used the available preliminary genomic sequence of A. ferrooxidans ATCC 23270 to isolate the DNA region containing the p21 gene. The nucleotide sequence of this DNA fragment contained a putative open reading frame (ORF) coding for a 23-kDa protein. This difference in size was due to the presence of a putative signal peptide in the ORF coding for P21. When p21 was cloned and overexpressed in Escherichia coli, the signal peptide was removed, resulting in a mature protein with a molecular mass of 21 kDa and a calculated isoelectric point of 9.18. P21 exhibited 27% identity and 42% similarity to the Deinococcus radiodurans thiosulfate-sulfur transferase (rhodanese; EC 2.8.1.1) and similar values in relation to other rhodaneses, conserving structural domains and an active site with a cysteine, both characteristic of this family of proteins. However, the purified recombinant P21 protein did not show rhodanese activity. Unlike cytoplasmic rhodaneses, P21 was located in the periphery of A. ferrooxidans cells, as determined by immunocytochemical analysis, and was regulated depending on the oxidizable substrate. The genomic context around gene p21 contained other ORFs corresponding to proteins such as thioredoxins and sulfate-thiosulfate binding proteins, clearly suggesting the involvement of P21 in inorganic sulfur metabolism in A. ferrooxidans.

Amino Acid Sequence↗