Thiosulfate reductase as a chlorate reductase inSalmonella typhimurium
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چکیده
منابع مشابه
Thiosulfate reductase isolated from Desulfotomaculum nigrificans.
A thiosulfate reductase from Desulfotomaculum nigrificans has been partially purified by ammonium sulfate fractionation, diethylaminoethylcellulose chromatography, and sucrose density gradient centrifugation. With inner-and outer-labeled (35)S-thiosulfate, the enzyme reduced only the outer sulfur atom to hydrogen sulfide. The enzyme was inhibited by sulfite and also by several sulfhydryl inhibi...
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A chlorate reductase has been purified from the chlorate-reducing strain Pseudomonas chloritidismutans. Comparison with the periplasmic (per)chlorate reductase of strain GR-1 showed that the cytoplasmic chlorate reductase of P. chloritidismutans reduced only chlorate and bromate. Differences were also found in N-terminal sequences, molecular weight, and subunit composition. Metal analysis and e...
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Strain GR-1 is one of several recently isolated bacterial species that are able to respire by using chlorate or perchlorate as the terminal electron acceptor. The organism performs a complete reduction of chlorate or perchlorate to chloride and oxygen, with the intermediate formation of chlorite. This study describes the purification and characterization of the key enzyme of the reductive pathw...
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Nitrate is one of the major sources of nitrogen for the growth of plants. It is taken up by plant roots and transported to the leaves where it is reduced to nitrite in the. The main objective of this research was to investigate stimulatory effects of sodium nitrate, potassium nitrate, ammonia and urea on the production/generation of the nitrate reductase mRNA in Triticum aestivum plants. The pl...
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The major inducible trimethylamine oxide reductase was purified from Salmonella typhimurium LT2. The molecular weights of the native enzyme were estimated to be 332,000 by gel filtration and 170,000 by nondenaturing disc gel electrophoresis. In sodium dodecyl sulfate-gel electrophoresis, the enzyme formed a single band of molecular weight 84,000. The isoelectric point was 4.28. Maximum activity...
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ژورنال
عنوان ژورنال: FEMS Microbiology Letters
سال: 1987
ISSN: 0378-1097,1574-6968
DOI: 10.1111/j.1574-6968.1987.tb02326.x