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'Nitrate Reductase' in keywords Facet   section ZfN Section C  [X]
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1984 (1)
1981 (1)
1980 (1)
1Author    CandadaiS. RamadossRequires cookie*
 Title    Effects of Vanadate on the Molybdoproteins Xanthine Oxidase and Nitrate Reductase: Kinetic Evidence for Multiple Site Interaction  
 Abstract    The inhibition of the activity o f xanthine oxidase by vanadate was strikingly similar to vanadate inhibition of another molybdoprotein nitrate reductase. Although the main catalytic activity of both enzymes was inhibited, the partial N AD H oxidase activity associated with these enzymes was stimulated several fold. It appears that the metal ion binds at multiple site in both enzymes. In the absence o f any enzymes a combination of vanadium (V) and molybdenum (V) in air was found to oxide NADH rapidly. 
  Reference    Z. Naturforsch. 35c, 702—707 (1980); received June 3 1980 
  Published    1980 
  Keywords    Molybdenum, Vanadium, Nitrate Reductase, Xanthine Oxidase 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0702.pdf 
 Identifier    ZNC-1980-35c-0702 
 Volume    35 
2Author    F. Castillo, F. J. Caballero, J. CárdenasRequires cookie*
 Title    Nitrate Photo-Assimilation by the Phototrophic Bacterium Rhodopseudomonas capsulata EjFj  
 Abstract    Rhodopseudomonas capsulata bacteria photo-assimilated nitrate under anaerobic condi­ tions, but were incapable of reducing it in the dark. The bacteria utilized dissolved N 2 as nitrogen source, but the growth in the presence o f nitrate was 5-fold higher. Nitrite was excreted to the medium, but not stoichiometrically with respect to nitrate consumption. Nitrate reductase is particulate and used reduced viologens or flavins as electron donors for nitrate reduction. The enzyme was inhibited in vitro by KCN, N aN 3, dithioerythritol and mercurials. Ammonia and other sources of reduced nitrogen repressed nitrate reductase synthesis. 
  Reference    Z. Naturforsch. 36c, 1025—1029 (1981); received July 30 1981 
  Published    1981 
  Keywords    Rhodopseudomonas capsulata EjFj, Nitrate, Nitrite, Nitrate Reductase, Photoassimilation 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-1025.pdf 
 Identifier    ZNC-1981-36c-1025 
 Volume    36 
3Author    S. G. Mauriño, M. A. Vargas, C. Echevarría, P.J A Paricio, J.M M AldonadoRequires cookie*
 Title    Red-Light Effects Sensitized by Methylene Blue on Nitrate Reductase from Spinach (Spinacia oleracea L.) Leaves  
 Abstract    Nitrate reductase from spinach (Spinacia oleracea L.) leaves, w hich had been inactivated in vitro by incubation with N A D H and cyanide, was fully reactivated in m inutes when irradiated in anaerobic conditions with red light in the presence o f m ethylene blue. Both the rate and the extent o f reactivation increased with light intensity (6 to 100 W -m " 2) and dye concentration (1 to 10 jiM). On the contrary, photoreactivation was com pletely abolished when N A D H or ethylenediaminetetra-acetic acid were present during irradiation. W e propose that m ethylene blue, when photo excited, exhibits a redox potential positive enough to reoxidise the CN~-re-duced molybdenum complex settled in the inactive enzym e, thus causing its reactivation. On the other hand, prolonged irradiation o f nitrate reductase, under air and in the presence o f methylene blue, promoted an oxygen-dependent irreversible inactivation o f the two partial activities o f the enzyme. This inactivation was m arkedly enhanced in 77% deuterated water and greatly prevented by azide, which indicates that singlet oxygen is the species primarily involved in the photooxidative inactivation o f the enzym e. 
  Reference    Z. Naturforsch. 39c, 1079—1084 (1984); received July 27 1984 
  Published    1984 
  Keywords    Methylene Blue, Nitrate Reductase, Photosensitization, Singlet O xygen, Spinacia 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-1079.pdf 
 Identifier    ZNC-1984-39c-1079 
 Volume    39