Bacillus stearothermophilus, membrane

Dissimilatory nitrate reductases (Pichinoty type A) in membrane fractions from bacteria have been shown capable of utilizing a variety of respiratory Intermediates and reduced pyridine nucleotides for nitrate reduction (Cole and Wimpeny, 1968 Knook et ai, 1973 Burke and Lascelles, 1975 Enoch and Lester, 1975). Reduction of nitrate by the membrane fractions, when respiratory substrates or pyridine nucleotides serve as reduc-tant, is generally inhibited by azide, cyanide and p-chloromercuribenzoate. Nitrate reduction, mediated by respiratory substrates, could be inhibited by n-heptylhydroxyquinoline-N oxide (HONO) or dicoumoral (Ruiz-Herrera and DeMoss, 1%9 Knook et al., 1973 Burke and Lascelles, 1975). However, in Micrococcus denitrificans (Lam and Nicholas, 1969) and in Bacillus stearothermophilus (Downey, 1%6) nitrate reduction is not inhibited by... 

Yamada and coworkers carried out characterization of a diaphorase monolayer at a glass surface in the same operationmode SECM [46]. Diaphorase purified from Bacillus stearothermophilus is a membrane protein, which catalyzes the oxidation of NADH in the presence of an electron mediator. Because of the high activity of diaphorase, a Michaelis-Menten type equation was applicable without further simplification for the boundary condition at the substrate surface. In the following studies [47], diaphorase patterns with monolayer-level coverage at flat glass substrates were visualized by feedback mode imaging. 

The formation of lipid-linked sugars in vitro by Bacillus stearothermophilus. Salmonella typhimurium, and Shigella jlexneri requires an unsaturated a-isoprenyl residue in a polyprenyl phosphate, in contrast to th- t in rat-liver microsomes which requires a saturated a-isoprenyl residue. o-Glucopyranosyl polyprenyl phosphate was formed on incubation of UDP-D-[ C]glucose with particulate preparations from B. stearothermophilus, and it may serve as a D-glucosyl donor in the synthesis of an extracellular polysaccharide. The properties of the membrane-associated sialyltransferase complexes of Escherichia coli have been examined. These complexes catalyse the incorporation of iV-acetylneuraminic... 

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