Results 381 to 390 of about 1,259,046 (413)
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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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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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, 1991
Inhibition of root elongation and modification of membrane properties are sensitive responses of plants to aluminium. The present paper reports on the effect of AI on lipid peroxidation and activities of enzymes related to production of activated oxygen ...
I. Cakmak, W. Horst
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Inhibition of root elongation and modification of membrane properties are sensitive responses of plants to aluminium. The present paper reports on the effect of AI on lipid peroxidation and activities of enzymes related to production of activated oxygen ...
I. Cakmak, W. Horst
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2015
Bacterial diheme peroxidases (bCCP) act in the detoxification of reactive oxygen species by reduction of peroxide to water. The substrate H2O2 is bound to the free axial position of a heme cofactor, and in a first step, one H2O molecule is released, while the remaining oxygen is stabilized as a metastable FeivO intermediate that awaits further ...
Brausemann, Anton +3 more
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Bacterial diheme peroxidases (bCCP) act in the detoxification of reactive oxygen species by reduction of peroxide to water. The substrate H2O2 is bound to the free axial position of a heme cofactor, and in a first step, one H2O molecule is released, while the remaining oxygen is stabilized as a metastable FeivO intermediate that awaits further ...
Brausemann, Anton +3 more
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Angewandte Chemie, 2015
The design and construction of efficient artificial enzymes is highly desirable. Recent studies have demonstrated that a series of carbon nanomaterials possess intrinsic peroxidase activity.
Hanjun Sun +5 more
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The design and construction of efficient artificial enzymes is highly desirable. Recent studies have demonstrated that a series of carbon nanomaterials possess intrinsic peroxidase activity.
Hanjun Sun +5 more
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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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Kinetics of glutathione peroxidase
Biochimica et Biophysica Acta (BBA) - Enzymology, 1969Abstract The dependency of the reaction rate of purified glutathione peroxidase (GSH: H2O2 oxidoreductase, EC 1.11.1.9) on the concentration of the substrates is investigated employing methods by which the substrates involved are determined immediately. GSH is measured polarographically. H2O2 is estimated by enzymatic oxidation of the fluorescent dye
Leopold Flohé, Ingeborg Brand
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Thiols as peroxidase substrates
Free Radical Biology and Medicine, 1993The abilities of haem peroxidases to catalyse the oxidation of various thiols were studied using the spin-trapping electron spin resonance (ESR) technique. Myeloperoxidase, a neutrophil and monocyte enzyme, catalysed the oxidation of cysteamine, cysteine methyl, and ethyl ester and to some extent 2-mercaptoethanol and thioglycollic acid.
Gunnel Ström +3 more
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Stereospecificity of horseradish peroxidase
Biological Chemistry, 2004We report here on the stereospecificity observed in the action of horseradish peroxidase (HRPC) on monophenol and diphenol substrates. Several enantiomers of monophenols and o-diphenols were assayed: L-tyrosinol, D-tyrosinol, L-tyrosine, DL-tyrosine, D-tyrosine, L-dopa, DL-dopa, D-dopa, L-alpha-methyldopa, DL-alpha-methyldopa, DL-adrenaline, D ...
José Tudela +6 more
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