Abstract:
:The open reading frame pp0053, which has a high homology with the sequence of mitochondrial sulfide dehydrogenase (HMT2) conferring cadmium tolerance in fission yeast, was amplified from Pseudomonas putida KT2440 and expressed in Escherichia coli JM109(DE3). The isolated and purified PP0053-His showed absorption spectra typical of a flavin adenine dinucleotide (FAD)--binding protein. The PP0053-His catalyzed a transfer of sulfide-sulfur to the thiophilic acceptor, cyanide, which decreased the Km value of the enzyme for sulfide oxidation and elevated the sulfide-dependent quinone reduction. Reaction of the enzyme with cyanide elicited a dose-dependent formation of a charge transfer band, and the FAD-cyanide adduct was supposed to work for a sulfur transfer. The pp0053 deletion from P. putida KT2440 led to activity declines of the intracellular catalase and ubiquinone-H2 oxidase. The sulfide-quinone oxidoreductase activity in P. putida KT2440 was attributable to the presence of pp0053, and the activity showed a close relevance to enzymatic activities related to sulfur assimilation.
journal_name
Can J Microbioljournal_title
Canadian journal of microbiologyauthors
Shibata H,Kobayashi Sdoi
10.1139/w06-022subject
Has Abstractpub_date
2006-08-01 00:00:00pages
724-30issue
8eissn
0008-4166issn
1480-3275pii
w06-022journal_volume
52pub_type
杂志文章abstract::Purification and chemical characterization of an immunosuppressive exopolysaccharide from Capnocytophaga ochracea strain 25 are described. This polysaccharide was extracted from spent culture medium by cold ethanol precipitation. Purification was accomplished by trichloroacetic acid and pronase treatments in combinati...
journal_title:Canadian journal of microbiology
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journal_title:Canadian journal of microbiology
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更新日期:2011-11-01 00:00:00
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更新日期:2007-12-01 00:00:00
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