Extension of Polyphenolics by CWPO-C Peroxidase Mutant Containing Radical-Robust Surface Active Site
نویسندگان
چکیده
منابع مشابه
Energetics of Cation Radical Formation at the Proximal Active Site Tryptophan of Cytochrome-c-Peroxidase and Ascorbate Peroxidase
Despite very similar protein structures, ascorbate peroxidase (APX) and yeast cytochrome-cperoxidase (CCP) stabilize different radical species during enzyme turnover. Both enzymes contain similar active site residues, including the tryptophan that is oxidized to a stable cation radical in CCP. However, the analogous trytophan is not oxidized in APX, and the second oxidizing equivalent is retain...
متن کاملFunctional mimicry of the active site of glutathione peroxidase by glutathione imprinted selenium-containing protein.
For imitating the active site of antioxidant selenoenzyme glutathione peroxidase (GPx), an artificial enzyme selenosubtilisin was employed as a scaffold for reconstructing substrate glutathione (GSH) specific binding sites by a bioimprinting strategy. GSH was first covalently linked to selenosubtilisin to form a covalent complex GSH-selenosubtilisin through a Se-S bond, then the GSH molecule wa...
متن کاملActive Site Mimicry of Glutathione Peroxidase by Glutathione Imprinted Selenium-Containing Trypsin
In order to overcome the instability of natural glutathione peroxidase (GPx), scientists endeavor to produce GPx mimics. The popular method first uses biological imprinting (BI) to produce the substrate binding sites and then employs chemical mutation (CM) to obtain the catalytic site. However, BICM has a drawback in that the catalytic site is not clear. Some researchers therefore tried to chan...
متن کاملEngineering the active site of ascorbate peroxidase.
The oxidation of a number of thioethers, namely methyl phenyl sulphide (1), ethyl phenyl sulphide (2), isopropyl phenyl sulphide (3), n-propyl phenyl sulphide (4), p-chlorophenyl methyl sulphide (5), p-nitrophenyl methyl sulphide (6) and methyl naphthalene sulphide (7), by recombinant pea cytosolic ascorbate peroxidase (rAPX) and a site-directed variant of rAPX in which the distal tryptophan 41...
متن کاملCatalytic surface radical in dye-decolorizing peroxidase: a computational, spectroscopic and site-directed mutagenesis study
Dye-decolorizing peroxidase (DyP) of Auricularia auricula-judae has been expressed in Escherichia coli as a representative of a new DyP family, and subjected to mutagenic, spectroscopic, crystallographic and computational studies. The crystal structure of DyP shows a buried haem cofactor, and surface tryptophan and tyrosine residues potentially involved in long-range electron transfer from bulk...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Applied Biochemistry and Biotechnology
سال: 2013
ISSN: 0273-2289,1559-0291
DOI: 10.1007/s12010-013-0534-2