Go toArchive
Browse byFacets
Bookbag ( 0 )
'Phototrophic Bacterium' in keywords
Results  2 Items
Sorted by   
Publication Year
1983 (1)
1982 (1)
1Author    Monier Habib, Tadros, Gerhart Drews, Dierk EversRequires cookie*
 Title    Peptidoglycan and Protein, the Major Cell Wall Constituents of the Obligate Halophilic Bacterium Rhodospirillum salexigens  
 Abstract    The obligate halophilic member o f Rhodospirillaceae, Rhodospirillum salexigens, does not con­ tain lipopolysaccharide in its thin and delicate gram-negative type cell wall. Major constituents are protein (approximately 70% of dry weight) and peptidoglycan (murein). 
  Reference    Z. Naturforsch. 37c, 210 (1982); received November 20 1981 
  Published    1982 
  Keywords    Murein, Peptidoglycan, Cell Wall, Halophilic, Phototrophic Bacterium, Protein 
  Similar Items    Find
 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0210.pdf 
 Identifier    ZNC-1982-37c-0210 
 Volume    37 
2Author    Michaela Preuß, Jobst-H Einrich KlemmeRequires cookie*
 Title    Purification and Characterization of a Dissimilatory Nitrite Reductase from the Phototrophic Bacterium Rhodopseudomonas palustris  
 Abstract    A dissimilatory nitrite reductase from the facultatively phototrophic bacterium , Rhodopseudo­ monas palustris strain la l was studied. A basic level o f the enzyme (1 0 -5 0 m U /m g protein) was measured in dark, aerated and anaerobic, photosynthetic cultures. A m arked derepression of enzyme synthesis occurred under conditions of oxygen lim itation (2 0 0 -3 0 0 m U /m g protein). The addition of nitrite (or nitrate) to the culture m edium had only a slight effect on the maximal nitrite reductase titer o f cells. The enzyme was purified from photosynthetically grown cells by precipitation with am m onium sulfate, gel filtration through Sepharose 6 B and repeated chromatography on DE 52-cellulose. As estimated by gel filtration, the nitrite reductase had a molecular weight o f about 120 000 + 12 000 and yielded only one band (mol. wt. o f about 68 000 + 7000) in SDS-gel electrophoresis. The isoelectric point o f the enzyme was at pH 5.1. Nitric oxide (NO) was identified as the reaction product of nitrite reduction. The enzyme also exhibited cytochrome c-oxidase activity and was active with chemically reduced viologen dyes, FMN and cytochrome c as electron donors. Highly purified nitrite reductase preparations con­ tained 10mol% of a c-type cytochrome. Trace metal analyses indicated the presence o f Cu in the enzyme. Consistent with the detection of Cu was the finding that the C u-chelator, diethyl-dithiocarbamate, strongly inhibited the nitrite reductase. 
  Reference    Z. Naturforsch. 38c, 933—938 (1983); received July 11/Septem ber 8 1983 
  Published    1983 
  Keywords    N itrite Reductase, N itrite D issimilation, Phototrophic Bacterium, Rhodopseudomonas palustris 
  Similar Items    Find
 TEI-XML for    default:Reihe_C/38/ZNC-1983-38c-0933.pdf 
 Identifier    ZNC-1983-38c-0933 
 Volume    38