نتایج جستجو برای: nitrate reductase activity

تعداد نتایج: 1188618  

Journal: :Journal of bacteriology 1987
D H Boxer D C Low J Pommier G Giordano

The soluble subcellular fraction of a chlB mutant contains an inactive precursor form of the molybdoenzyme nitrate reductase, which can be activated by the addition to the soluble fraction of protein FA, which is thought to be the active product of the chlB locus. Dialysis or desalting of the chlB soluble fraction leads to the loss of nitrate reductase activation, indicating that some low-molec...

Journal: :The Biochemical journal 1999
L C Potter J A Cole

The seven nap genes at minute 47 on the Escherichia coli K-12 chromosome encode a functional nitrate reductase located in the periplasm. The molybdoprotein, NapA, is known to be essential for nitrate reduction. We now demonstrate that the two c-type cytochromes, the periplasmic NapB and the membrane-associated NapC, as well as a fourth polypeptide, NapD, are also essential for nitrate reduction...

Journal: :Journal of bacteriology 1992
C L Santini C Iobbi-Nivol C Romane D H Boxer G Giordano

All molybdoenzyme activities are absent in chlB mutants because of their inability to synthesize molybdopterin guanine dinucleotide, which together with molybdate constitutes the molybdenum cofactor in Escherichia coli. The chlB mutants are able to synthesize molybdopterin. We have previously shown that the inactive nitrate reductase present in a chlB mutant can be activated in a process requir...

2008
Celedonio Gonzalez Gregorio Gonzalez Julio Avila M. Dolores Perez Nelida Brito Jose M. Siverio

Laguna, Tenerife, Canarias, Spain haemand Mo-dependent and Mo-dependent activities of nitrate reductase, determined with the non-physiological electron donors FMNH, and reduced methyl viologen respectively, were less affected. A similar inactivation was found with the proton ionophores 2,rddinitrophenol and carbonyl cyanide m-chlorophenylhydrazone. The inactive enzyme was found in the particula...

2005

1. In rice seedlings synthesis of methyl viologen-nitrite reductase was stimulated by light, as was that of NADH-nitrate oxidoreductase (EC 1.6.6.1). A small residual effect of light on the synthesis of the enzymes persisted in the dark for a short time. 2. In etiolated seedlings exposed to light and nitrate, a lag period of 3 h was necessary before enzyme synthesis commenced, whereas in green ...

Journal: :The Journal of biological chemistry 1986
M J Barber L P Solomonson

Incubation of the complex metalloflavoprotein, assimilatory nitrate reductase with N-ethylmaleimide, or a spin-labeled analog, 4-maleimido-2,2,6,6-tetramethylpiperidinooxyl, resulted in a time-dependent inactivation of NADH:nitrate reductase and NADH: cytochrome-c reductase activity with no effect on reduced methyl viologen:nitrate reductase activity. Inactivation of the enzyme, which could be ...

Journal: :Genetics 1988
C Klittich J F Leslie

Twelve strains of Fusarium moniliforme were examined for their ability to sector spontaneously on toxic chlorate medium. All strains sectored frequently; 91% of over 1200 colonies examined formed chlorate-resistant, mutant sectors. Most of these mutants had lesions in the nitrate reduction pathway and were unable to utilize nitrate (nit mutants). nit mutations occurred in seven loci: a structur...

Journal: :Journal of bacteriology 1999
H Wang C P Tseng R P Gunsalus

Escherichia coli synthesizes two biochemically distinct nitrate reductase enzymes, a membrane-bound enzyme encoded by the narGHJI operon and a periplasmic cytochrome c-linked nitrate reductase encoded by the napFDAGHBC operon. To address why the cell makes these two enzymes, continuous cell culture techniques were used to examine napF and narG gene expression in response to different concentrat...

2013
udrun D. Trogisch W olfram R. Ullrich

G udrun D. Trogisch*, H elm ut Köcher**, and W olfram R. Ullrich* * Institut für Botanik, Technische Hochschule, Schnittspahnstraße 3. D-6100 Darmstadt, Bundesrepublik Deutschland ** Hoechst AG, D-6230 Frankfurt 80. Bundesrepublik Deutschland Z. Naturforsch. 44c, 33 — 38 (1989); received July 13/November 11, 1988 Dedicated to Professor Wilhelm Simonis on the occasion o f his 80th birthday Ammon...

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