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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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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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Looking for syringyl peroxidases
Trends in Plant Science, 2007Lignins are cell wall heteropolymers that arise from the peroxidase-mediated coupling of p-coumaryl, coniferyl and sinapyl alcohols. In gymnosperms, they are derived from coniferyl alcohol, whereas in angiosperms, lignins are derived from coniferyl and sinapyl alcohols. Thus, although it is frequently assumed that the chemical complexity of lignins has
Alfonso Ros Barceló +2 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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Iodination by thyroid peroxidase
1984Publisher Summary The Iodination of tyrosyl moieties in thyroglobulin and other proteins is catalyzed by the thyroid peroxidase (TPO), an integral membrane, heme glycoprotein. Tyrosine and tyrosyl peptides can also be iodinated by TPO. The iodination reaction requires H 2 O 2 , I - , an enzyme-associated iodinating intermediate (TPO-I oxid ), and an ...
J T Neary, Farahe Maloof, Morris Soodak
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The glutathione peroxidase family: Discoveries and mechanism.
Free Radical Biology & Medicine, 2022L. Flohé, S. Toppo, L. Orian
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1985
Catalase is the enzyme that catalyzes the decomposition of hydrogen peroxide to water and dioxygen. The usual sources of catalase are bovine liver and bovine erythrocytes. The enzyme exists as a 250,000–dalton tetramer with one heme per monomer. The complete amino acid sequence of the bovine liver enzyme is known (Schroeder et al., 1982) as well as ...
Damon L. Meyer, Llyod L. Ingraham
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Catalase is the enzyme that catalyzes the decomposition of hydrogen peroxide to water and dioxygen. The usual sources of catalase are bovine liver and bovine erythrocytes. The enzyme exists as a 250,000–dalton tetramer with one heme per monomer. The complete amino acid sequence of the bovine liver enzyme is known (Schroeder et al., 1982) as well as ...
Damon L. Meyer, Llyod L. Ingraham
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Enzymatic hydrolysis of corn stover lignin by laccase, lignin peroxidase, and manganese peroxidase.
Bioresource Technology, 2022Sitong Zhang +7 more
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