Results 261 to 270 of about 48,716 (304)
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Biotransformations with Peroxidases
1999Enzymes are chiral catalysts and are able to produce optically active molecules from prochiral or racemic substrates by catalytic asymmetric induction. One of the major challenges in organic synthesis is the development of environmentally acceptable chemical processes for the preparation of enantiomerically pure compounds, which are of increasing ...
W, Adam +6 more
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Cellular and Molecular Life Sciences, 2001
There are several proteins in mammalian cells that can metabolize hydrogen peroxide and lipid hydroperoxides. These proteins include four selenium-containing glutathione peroxidases that are found in different cell fractions and tissues of the body. This review considers the structure and distribution of the selenoperoxidases and how this relates to ...
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There are several proteins in mammalian cells that can metabolize hydrogen peroxide and lipid hydroperoxides. These proteins include four selenium-containing glutathione peroxidases that are found in different cell fractions and tissues of the body. This review considers the structure and distribution of the selenoperoxidases and how this relates to ...
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Free Radical Research, 2015
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Hawkins, Clare C.L. +1 more
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Hawkins, Clare C.L. +1 more
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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
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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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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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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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Lignin peroxidase-type activity of soybean peroxidase
Enzyme and Microbial Technology, 1995Soybean peroxidase (SBP), an acidic peroxidase isolated from the hulls of the bean, catalyzes the efficient oxidation of veratryl alcohol to veratraldehyde in the presence of H2O2. The reaction is optimal at pH 2.4 in the presence of 0.2 m CaCl2. Soybean peroxidase is highly thermostable at pH 2.4, with half-lives of 210 and 2.5 h at 30 and 50°C ...
James P. McEldoon +2 more
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Archives of Biochemistry and Biophysics, 1952
Abstract The evidence for horse-radish peroxidase heme linkages has been reinvestigated in the acid region and there no longer exists experimental support for a heme-linked hydroxyl group. The formation of inactive compound B and the splitting of the enzyme terminate the activity of the enzyme.
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Abstract The evidence for horse-radish peroxidase heme linkages has been reinvestigated in the acid region and there no longer exists experimental support for a heme-linked hydroxyl group. The formation of inactive compound B and the splitting of the enzyme terminate the activity of the enzyme.
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The Oxidation of Bilirubin by Peroxidase
Science, 1945J B, Sumner, M, Nymon
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