Engineering a horseradish peroxidase C stable to radical attacks by mutating multiple radical coupling sites
نویسندگان
چکیده
منابع مشابه
Production of the superoxide radical by horseradish peroxidase.
The reaction mixture contained, in a total volume of 1.00m1, enzyme, p-coumaric acid (2.5pmol), dihydroxyfumaric acid (30pmol), KH2P04 (8.3pmol) and sufficient KOH to adjust the pH to 6. Incubations were carried out for 0.5h at 25°C and caffeic acid production was assayed as described by Halliwell(l975). 100% corresponded to a rate of 60nmol of caffeic acid formed in 0.5h. Oxidation of dihydrox...
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This paper reports the free radical polymerization of methyl methacrylate (MMA) catalyzed by horseradish peroxidase (HRP). A novel method was developed whereby MMA polymerization can be carried out at ambient temperatures in the presence of low concentrations of hydrogen peroxide and 2,4-pentanedione in a mixture of water and a water-miscible solvent. Polymers of MMA formed were highly stereore...
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Phagocytes secrete the heme protein myeloperoxidase, which is present and active in human atherosclerotic tissue. These cells also generate hydrogen peroxide (H2O2), thereby allowing myeloperoxidase to generate a range of oxidizing intermediates and stable end products. When this system acts on L-tyrosine in vitro, it forms o, o'-dityrosine, which is enriched in atherosclerotic lesions. Myelope...
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Article history: Received 14 May 2015 Received in revised form 5 July 2015 Accepted 8 July 2015 Available online 9 July 2015 Graphene-based nanomaterials have been widely studied as high-performance matrices for enzyme immobilization and in the development of biosensors. Surface O-functionalities of graphene induce changes in chemical reactivity and electronic conductivity of nanomaterials and ...
متن کاملChemical nature of the porphyrin pi cation radical in horseradish peroxidase compound I.
The electron paramagnetic resonance (EPR) and Mössbauer properties of native horseradish peroxidase have been compared with those of a synthetic derivative of the enzyme in which a mesohemin residue replaces the natural iron protoporphyrin IX heme prosthetic group. The oxyferryl pi cation radical intermediate, compound I, has been formed from both the native and synthetic enzyme, and the magnet...
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ژورنال
عنوان ژورنال: Biotechnology and Bioengineering
سال: 2014
ISSN: 0006-3592
DOI: 10.1002/bit.25483