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<span style = 'font-size: large'> '''Tsang, ML and Schiff, JA'''  (1976) Sulfate-reducing pathway in Escherichia coli involving bound intermediates.''J. Bacteriol.'' '''125''':923-33</span>
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!align=left  |Citation
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'''Tsang, ML and Schiff, JA'''  (1976) Sulfate-reducing pathway in Escherichia coli involving bound intermediates. ''J. Bacteriol.'' '''125''':923-33
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!align=left  |Abstract
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Although a sulfate-reducing pathway in Escherichia coli involving free sulfite and sulfide has been suggested, it is shown that, as in Chlorella, a pathway involving bound intermediates is also present. E. coli extracts contained a sulfotransferase that transferred the sulfonyl group from a nucleosidephosphosulfate to an acceptor to form an organic thiosulfate. This enzyme was specific for adenosine 3'-phosphate 5'-phosphosulfate, did not utilize adenine 5'-phosphosulfate, and transferred to a carrier molecule that was identical with thioredoxin in molecular weight and amino acid composition. In the absence of thioredoxin, only very low levels of the transfer of the sulfo group to thiols was observed. As in Chlorella, thiosulfonate reductase activity that reduced glutathione-S-SO3- to bound sulfide could be detected. In E. coli, this enzyme used reduced nicotinamide adenine dinucleotide phosphate and Mg2+, but did not require the addition of ferredoxin or ferredoxin nicotinamide adenine dinucleotide phosphate reductase. Although in Chlorella the thiosulfonate reductase appears to be a different enzyme from the sulfite reductase, the E. coli thiosulfonate reductase and sulfite reductase may be activities of the same enzyme.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=3497 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC236168 PMC236168]


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|{{TableHeadingColor}} |'''Abstract''' || Although a sulfate-reducing pathway in Escherichia coli involving free sulfite and sulfide has been suggested, it is shown that, as in Chlorella, a pathway involving bound intermediates is also present. E. coli extracts contained a sulfotransferase that transferred the sulfonyl group from a nucleosidephosphosulfate to an acceptor to form an organic thiosulfate. This enzyme was specific for adenosine 3'-phosphate 5'-phosphosulfate, did not utilize adenine 5'-phosphosulfate, and transferred to a carrier molecule that was identical with thioredoxin in molecular weight and amino acid composition. In the absence of thioredoxin, only very low levels of the transfer of the sulfo group to thiols was observed. As in Chlorella, thiosulfonate reductase activity that reduced glutathione-S-SO3- to bound sulfide could be detected. In E. coli, this enzyme used reduced nicotinamide adenine dinucleotide phosphate and Mg2+, but did not require the addition of ferredoxin or ferredoxin nicotinamide adenine dinucleotide phosphate reductase. Although in Chlorella the thiosulfonate reductase appears to be a different enzyme from the sulfite reductase, the E. coli thiosulfonate reductase and sulfite reductase may be activities of the same enzyme.
!align=left  |Keywords
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Cell-Free System; Electron Transport; Escherichia coli/enzymology; Escherichia coli/metabolism; Glutathione/metabolism; Models, Biological; NADP/metabolism; Nucleotidases/metabolism; Oxidation-Reduction; Oxidoreductases/metabolism; Phosphoadenosine Phosphosulfate/metabolism; Phosphoric Monoester Hydrolases/metabolism; Sulfates/metabolism; Sulfites/metabolism; Sulfurtransferases/metabolism; Thioredoxins/metabolism
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=3497 PubMed]
 
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Latest revision as of 04:46, 15 September 2013

Citation

Tsang, ML and Schiff, JA (1976) Sulfate-reducing pathway in Escherichia coli involving bound intermediates. J. Bacteriol. 125:923-33

Abstract

Although a sulfate-reducing pathway in Escherichia coli involving free sulfite and sulfide has been suggested, it is shown that, as in Chlorella, a pathway involving bound intermediates is also present. E. coli extracts contained a sulfotransferase that transferred the sulfonyl group from a nucleosidephosphosulfate to an acceptor to form an organic thiosulfate. This enzyme was specific for adenosine 3'-phosphate 5'-phosphosulfate, did not utilize adenine 5'-phosphosulfate, and transferred to a carrier molecule that was identical with thioredoxin in molecular weight and amino acid composition. In the absence of thioredoxin, only very low levels of the transfer of the sulfo group to thiols was observed. As in Chlorella, thiosulfonate reductase activity that reduced glutathione-S-SO3- to bound sulfide could be detected. In E. coli, this enzyme used reduced nicotinamide adenine dinucleotide phosphate and Mg2+, but did not require the addition of ferredoxin or ferredoxin nicotinamide adenine dinucleotide phosphate reductase. Although in Chlorella the thiosulfonate reductase appears to be a different enzyme from the sulfite reductase, the E. coli thiosulfonate reductase and sulfite reductase may be activities of the same enzyme.

Links

PubMed PMC236168

Keywords

Cell-Free System; Electron Transport; Escherichia coli/enzymology; Escherichia coli/metabolism; Glutathione/metabolism; Models, Biological; NADP/metabolism; Nucleotidases/metabolism; Oxidation-Reduction; Oxidoreductases/metabolism; Phosphoadenosine Phosphosulfate/metabolism; Phosphoric Monoester Hydrolases/metabolism; Sulfates/metabolism; Sulfites/metabolism; Sulfurtransferases/metabolism; Thioredoxins/metabolism

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