Results 351 to 360 of about 1,308,579 (395)
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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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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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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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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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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
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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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Journal of Experimental Botany, 1979
Kinetin and a,a'-dipyridyl prevented the rapid decrease of chlorophyll content in detached oat leaves senescing in the dark. In the light, detachment caused a 27-40% rise in peroxidase activity and kinetin enhanced the enzyme in the segments by about 80%.
J. Goldstein +2 more
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Kinetin and a,a'-dipyridyl prevented the rapid decrease of chlorophyll content in detached oat leaves senescing in the dark. In the light, detachment caused a 27-40% rise in peroxidase activity and kinetin enhanced the enzyme in the segments by about 80%.
J. Goldstein +2 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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Structural properties of peroxidases
Journal of Biotechnology, 1997Peroxidases are heme proteins which are able to catalyze the oxidation of a large variety of substrates through the reaction with hydrogen peroxide. The specific biological function, the reduction potential of the iron and the nature of the substrates which can be oxidized, are strongly determined by the structural features of the protein matrix around
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Oxidation states of peroxidase
Molecular and Cellular Biochemistry, 1973Five oxidation states of horseradish peroxidase, ferrous, ferric, Compounds I and II, oxy-ferrous, are known. Various reactions and plausible structures of these states are reported. Mechanisms of peroxidase-oxidase reactions are discussed in terms of the five oxidation states of the enzyme.
Ken-nosuke Yokota, Isao Yamazaki
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