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Query: EC:1.7.1.2 (nitrate reductase)
 3,861 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The observation that oxygen represses nitrate reductase biosynthesis in a hemA mutant grown aerobically with or without delta-aminolevulinic acid indicates that cytochromes are not responsible for nitrate reductase repression in aerobically grown cells.
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PMID:Do cytochromes function as oxygen sensors in the regulation of nitrate reductase biosynthesis? 32 68

Membrane-bound nitrate reductase of Escherichia coli consists of three subunits designated as A, B, and C, with subunit C being the apoprotein of cytochrome b, A hemA mutant that cannot synthesize delta-aminolevulinic acid (ALA) produces a normal, stable, membrane-bound enzyme when grown with ALA. When grown without ALA, this mutant makes a reduced amount of membrane-bound enzyme that is unstable and contains no C subunit. Under the same growth conditions, this mutant accumulates a large amount of a soluble form of the enzyme in the cytoplasm. Accumulation of this cytoplasmic form begins immediately upon induction of the enzyme with nitrate. The cytoplasmic form is very similar to the soluble form of the enzyme obtained by alkaline heat extraction. It is a high-molecular-weight complex with a Strokes radius of 8.0 nm and consists of intact A and B subunits. When ALA is added to a culture growing without ALA, the cytoplasmic form of the enzyme is incorporated into the membrane in a stable form, coincident with the formation of functional cytochrome b. Reconstitution experiments indicate that subunit C is present in cultures grown without ALA but is reduced in amount or unstable. These results indicate that membrane-bound nitrate reductase is synthesized via a soluble precursor containing subunits A and B, which then binds to the membrane upon interaction with the third subunit, cytochrome b.
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PMID:Biosynthesis of membrane-bound nitrate reductase in Escherichia coli: evidence for a soluble precursor. 77 Apr 17

Mutants H-14 and H-18 of Staphylococcus aureus require hemin for growth on glycerol and other nonfermentable substrates. H-14 also responds to delta-aminolevulinate. Heme-deficient cells grown in the presence of nitrate do not have lactate-nitrate reductase activity but gain this activity when incubated with hemin in buffer and glucose. Lactate-nitrate reductase activity is also restored to the membrane fraction from such cells by incubation with hemin and dithiothreitol; addition of adenosine 5'-triphosphate has no effect upon the restoration. Cells grown with nitrate in the absence of hemin have two to five times more reduced benzyl viologen-nitrate reductase activity than do those grown with hemin. The activity increases throughout the growth period in the absence of hemin, but with hemin present enzyme formation ceases before the end of growth. There was no evidence of enzyme destruction. The distribution of nitrate reductase activity between membrane and cytoplasm was similar in cells grown with and without hemin; 70 to 90% was in the cytoplasm. It is concluded that heme-deficient staphylococci form apo-cytochrome b, which readily combines in vitro with its prosthetic group to restore normal function. The avaliability of the heme prosthetic group influences the formation of nitrate reductase.
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PMID:Nitrate reductase activity in heme-deficient mutants of Staphylococcus aureus. 126 3

Plants of Nymphaea alba L. grown at various levels of chromium (VI) ranging from 1 to 200 microM accumulated chromium in concentration and duration-dependent manner. At all Cr levels, chromium accumulation by various plant tissues followed the order roots > leaves > rhizomes. Approximately 93% of total chromium present in the medium was accumulated by plants at lowest conentration (1 microM) used in the experiment. Chromium-induced toxicity appears at 1 microM chromium resulting in the build-up of delta-aminolevulinic acid (ALA) and reduced activities of delta-aminolevulinic acid dehydratase (ALAD) and nitrate reductase (NR), total chlorophyll (Chl) and protein contents. Ch1a was more sensitive than Ch1b to chromium toxicity. It could be inferred that chromium toxicity is not located at the level of ALA synthesis, but, probably at the ALAD activity which was more severely affected during chlorophyll biosynthesis. Finally, impaired chlorophyll biosynthesis resulted in reduced total chlorophyll content.
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PMID:Chromium (VI) accumulation reduces chlorophyll biosynthesis, nitrate reductase activity and protein content in Nymphaea alba L. 1087 26