Biochemical and Genetic Characterization of nirB Mutants of Escherichia coli K12 Pleiotropically Defective in Nitrite and Sulphite Reduction

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Biochemical and genetic characterization of nirB mutants of Escherichia coli K 12 pleiotropically defective in nitrite and sulphite reduction.

Mutants of Escherichia coli K12 defective in the nirB gene lack NADH-dependent nitrite reductase activity and reduce nitrite slowly during anaerobic growth. With one exception these mutants require cysteine for growth. Cytochrome C552 synthesis and the assimilation of ammonia are unaffected by the nirB mutation. The defective gene is located between the crp and aroB genes at minute 73 on the E...

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Isolation and characterization of cysK mutants of Escherichia coli K12.

cysK mutants, deficient in O-acetylserine sulphydrylase A [O-acetyl-L-serine acetate-lyase (adding hydrogen-sulphide); EC 4.2.99.8], were isolated as strains resistant to selenite or giving a black colour reaction on bismuth citrate indicator medium. All were resistant to the inhibitor I,2,4-triazole. Four independent mutants were found which possessed lowered levels of O-acetylserine sulphydry...

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Mutants of Salmonella typhimurium and Escherichia coli pleiotropically defective in active transport.

Two classes of mutants isolated from E. coli and Salmonella typhimurium are altered in respiration-coupled active transport, as studied in whole cells and/or isolated membrane vesicles. Mutant cells defective in D-lactate dehydrogenase (dld) transport amino acids and lactose normally. Membrane vesicles prepared from these mutants do not exhibit D-lactate-dependent transport, D-lactate oxidation...

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extraction and characterization of allium irancum plant extract and its application in the green synthesis of silver nano particles and oxidation of thiocarbony1 compounds

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Purification and properties of nitrite reductase from Escherichia coli K12.

NADH-nitrite oxidoreductase (EC 1.6.4) was purified to better than 95% homogeneity from batch cultures of Escherichia coli strain OR75Ch15, which is partially constitutive for nitrite reductase synthesis. Yields of purified enzyme were low, mainly because of a large loss of activity during chromatography on DEAE-cellulose. The quantitative separation of cytochrome c-552 from nitrite reductase a...

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ژورنال

عنوان ژورنال: Microbiology

سال: 1980

ISSN: 1350-0872,1465-2080

DOI: 10.1099/00221287-120-2-475