Results 371 to 380 of about 1,259,046 (413)
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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 ...
Alan J. Gengenbach +3 more
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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 ...
Alan J. Gengenbach +3 more
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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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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.
Yihui Hu +9 more
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ACS Nano, 2019
The work describes a carbon-based peroxidase mimic, N- and B-codoped reduced graphene oxide (NB-rGO), which shows high peroxidase-like activity without oxidase-like activity and has a catalytic efficiency nearly 1000-fold higher than that of undoped rGO.
M. Kim +6 more
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The work describes a carbon-based peroxidase mimic, N- and B-codoped reduced graphene oxide (NB-rGO), which shows high peroxidase-like activity without oxidase-like activity and has a catalytic efficiency nearly 1000-fold higher than that of undoped rGO.
M. Kim +6 more
semanticscholar +1 more source
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 ...
Alexander R. Pokora +2 more
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Molecular and Cellular Biochemistry, 1988
It is well known that the partial reduction of oxygen can result in the formation of highly reactive oxygen products. Hydrogen peroxide is one of these metabolites of oxygen. Peroxidases utilize this metabolite for a variety of functions. It is the purpose of this treatise to review the nature and function of various membrane peroxidases in the body.
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It is well known that the partial reduction of oxygen can result in the formation of highly reactive oxygen products. Hydrogen peroxide is one of these metabolites of oxygen. Peroxidases utilize this metabolite for a variety of functions. It is the purpose of this treatise to review the nature and function of various membrane peroxidases in the body.
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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.
Tsunehisa Araiso, H. Brian Dunford
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2010
The human peroxidases are hemoproteins that utilize H2O2 to oxidize a variety of endogenous and exogenous substrates. The well-established members of this enzyme family are eosinophil peroxidase, lactoperoxidase, myeloperoxidase, and thyroid peroxidase.
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The human peroxidases are hemoproteins that utilize H2O2 to oxidize a variety of endogenous and exogenous substrates. The well-established members of this enzyme family are eosinophil peroxidase, lactoperoxidase, myeloperoxidase, and thyroid peroxidase.
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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 ...
Florian Rüker +6 more
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Arabidopsis thalianaperoxidase N: structure of a novel neutral peroxidase
Acta Crystallographica Section D Biological Crystallography, 2000The structure of the neutral peroxidase from Arabidopsis thaliana (ATP N) has been determined to a resolution of 1.9 A and a free R value of 20.5%. ATP N has the expected characteristic fold of the class III peroxidases, with a C(alpha) r.m.s.d. of 0.82 A when compared with horseradish peroxidase C (HRP C).
Mirza, Osman Asghar +4 more
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