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Heavy Metals in Elecronic Cigarette Aersol Can Accumulate in Lung Epithelial Cells [PDF]
, 2019 Zaman, Rafay
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The structure of the flavoenzyme glutathione reductase [PDF]
Nature, 1978 The three-dimensional structure of the dimeric flavoenzyme glutathione reductase from human erythrocytes has been elucidated by an X-ray diffraction analysis at 0.3 nm resolution. The polypeptide chain has been traced, and the binding positions of FAD, NADP and glutathione have been determined. A mechanism for the electron transfer is discussed.
Schulz, G. +3 more
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Glutathione reductase in evolution
Journal of Molecular Evolution, 1983The disulfide reducing activities of GSSG-and CoASSG-reductases were measured on partially purified extracts from a variety of prokaryotes and eukaryotes. Glutathione-reductase was found in varying amounts in all eukaryotes and prokaryotes, used in this study, with the exception of the two strict anaerobes Clostridium tartarivorum and Desulfovibrio ...
M. Ondarza, R. N. Ondarza, J. L. Rendón
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Inhibition of glutathione disulfide reductase by glutathione
Archives of Biochemistry and Biophysics, 1991Rat-liver glutathione disulfide reductase is significantly inhibited by physiological concentrations of the product, glutathione. GSH is a noncompetitive inhibitor against GSSG and an uncompetitive inhibitor against NADPH at saturating concentrations of the fixed substrate.
Hiram F. Gilbert +2 more
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Proteins: Structure, Function, and Bioinformatics, 2008
AbstractThioredoxin glutathione reductase (TGR) is a key flavoenzyme expressed by schistosomes that bridges two detoxification pathways crucial for the parasite survival in the host's organism. In this article we report the crystal structure (at 2.2 Å resolution) of TGR from Schistosoma mansoni (SmTGR), deleted in the last two residues.
ANGELUCCI, Francesco +5 more
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AbstractThioredoxin glutathione reductase (TGR) is a key flavoenzyme expressed by schistosomes that bridges two detoxification pathways crucial for the parasite survival in the host's organism. In this article we report the crystal structure (at 2.2 Å resolution) of TGR from Schistosoma mansoni (SmTGR), deleted in the last two residues.
ANGELUCCI, Francesco +5 more
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Reduction of a Trisulfide Derivative of Glutathione by Glutathione Reductase
Biochemical and Biophysical Research Communications, 1994Glutathione trisulfide was synthesized from glutathione disulfide and its reduction by glutathione reductase was studied. A two-step reaction was observed. In a first step, the rate of reduction was similar to that observed with glutathione disulfide.
Moutiez, M. +5 more
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Inhibition of glutathione reductase by oncomodulin
Archives of Biochemistry and Biophysics, 1990Evidence for a specific interaction between oncomodulin and glutathione reductase is presented. Glutathione reductase (EC 1.6.4.2) isolated from either the bovine intestinal mucosa or the rat liver was bound in a Ca2(+)-dependent manner to oncomodulin which was covalently attached to Sepharose.
Palmer, E., Macmanus, J., Mutus, B.
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Ageing of Glutathione Reductase in the Lens
Experimental Eye Research, 1994The distribution of glutathione reductase activity in concentric layers from the lens has been determined as a function of age for 16 species. Primate lenses have almost ten times the level of glutathione reductase found in other species. Comparison with the activity of hexokinase revealed that this is not due to a higher overall rate of metabolism in ...
Robert C. Augusteyn, Wei Zheng Zhang
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Interaction of nitrofurans with glutathione reductase
Biochimica et Biophysica Acta (BBA) - General Subjects, 1991Nitrofurans inhibit the oxidation of NADPH by glutathione, catalyzed by yeast glutathione reductase (EC 1.6.4.2). acting as uncompetitive incomplete inhibitors for NADPH and glutathione. The quinoline-substituted nitrofurans were the most effective inhibitors.
Juozas J. Kulys +3 more
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Glutathione reductase functions as vanadate(V) reductase
Archives of Biochemistry and Biophysics, 1990The oxidation of NADPH by vanadate(V) in the presence of glutathione reductase showed typical enzymatic kinetics. The oxidation was inhibited by N-ethylmaleimide, a glutathione reductase inhibitor. Superoxide dismutase had no significant effect on the oxidation, indicating noninvolvement of the superoxide radical. The vanadate(V) reduction was found to
Naresh S. Dalal, Xianglin Shi
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