Results 301 to 310 of about 1,072,450 (362)
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Catalytically Synthesized Prussian Blue Nanoparticles Defeating Natural Enzyme Peroxidase.
Journal of the American Chemical Society, 2018We synthesized Prussian Blue (PB) nanoparticles through catalytic reaction involving hydrogen peroxide (H2O2) activation. The resulting nanoparticles display the size-dependent catalytic rate constants in H2O2 reduction, which are significantly improved ...
M. Komkova, E. E. Karyakina, A. Karyakin
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Applied Microbiology and Biotechnology, 2014
The white-rot fungus Phanerochaete chrysosporium secretes extracellular oxidative enzymes during secondary metabolism, but lacks versatile peroxidase, an enzyme important in ligninolysis and diverse biotechnology processes. In this study, we report the genetic modification of a P.
Nancy, Coconi-Linares +5 more
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The white-rot fungus Phanerochaete chrysosporium secretes extracellular oxidative enzymes during secondary metabolism, but lacks versatile peroxidase, an enzyme important in ligninolysis and diverse biotechnology processes. In this study, we report the genetic modification of a P.
Nancy, Coconi-Linares +5 more
openaire +2 more sources
Nitrogen-Doped Carbon Nanomaterials as Highly Active and Specific Peroxidase Mimics
Chemistry of Materials, 2018Nanozymes, the enzyme-mimicking nanomaterials, have been developed to overcome the low stability and high cost of natural enzymes. Unlike highly active and specific enzymes, however, the catalytic activities of nanozymes are moderate and lack specificity.
Yi-Hui Hu +9 more
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Biochemistry, 1999
Trp191Phe and Trp51Phe mutations have been introduced into an engineered cytochrome c peroxidase (CcP) containing a Mn(II)-binding site reported previously (MnCcP; see Yeung, B. K.-S., et al. (1997) Chem. Biol. 5, 215-221). The goal of the present study is to elucidate the role of tryptophans in peroxidase activity since CcP contains both Trp51 and ...
A, Gengenbach, S, Syn, X, Wang, Y, Lu
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Trp191Phe and Trp51Phe mutations have been introduced into an engineered cytochrome c peroxidase (CcP) containing a Mn(II)-binding site reported previously (MnCcP; see Yeung, B. K.-S., et al. (1997) Chem. Biol. 5, 215-221). The goal of the present study is to elucidate the role of tryptophans in peroxidase activity since CcP contains both Trp51 and ...
A, Gengenbach, S, Syn, X, Wang, Y, Lu
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Horseradish peroxidase. XXXVI. On the difference between peroxidase and metmyoglobin
Biochemical and Biophysical Research Communications, 1979Abstract A mechanism for the reaction of hydrogen peroxide with horseradish peroxidase is proposed which involves the catalytic activity of the carboxylate side chain of aspartate residue 43. The corresponding residue in the active site of metmyoglobin is glycine E8, which explains the inability of metmyoglobin to form compound I.
H B, Dunford, T, Araiso
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Catalase-Peroxidases in Cyanobacteria – Similarities and Differences to Ascorbate Peroxidases
Free Radical Research, 1999Cyanobacteria (blue-green algae) are oxygenic phototrophic bacteria carrying out plant-type photosynthesis. The only hydrogen peroxide scavenging enzymes in at least two unicellular species have been demonstrated to be bifunctional cytosolic catalase-peroxidases (CatPXs) having considerable homology at the active site with plant ascorbate peroxidases ...
C, Obinger +6 more
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Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase.
Journal of Laboratory and Clinical Medicine, 1967D. Paglia, W. N. Valentine
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Assays of glutathione peroxidase.
Methods in Enzymology, 1984Leopold Flohé, W. Günzler
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Selenium: Biochemical Role as a Component of Glutathione Peroxidase
Science, 1973J. T. Rotruck +5 more
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Hydrogen Peroxide is Scavenged by Ascorbate-specific Peroxidase in Spinach Chloroplasts
, 1981Y. Nakano, K. Asada
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