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1دورية أكاديمية
المؤلفون: Lin, Kuan‐Hung, Lyu, Syue‐Yi, Yeh, Hsien‐Wei, Li, Yi‐Shan, Hsu, Ning‐Shian, Huang, Chun‐Man, Wang, Yung‐Lin, Shih, Hao‐Wei, Wang, Zhe‐Chong, Wu, Chang‐Jer, Li, Tsung‐Lin
المصدر: Protein Science. 29(7)
مصطلحات موضوعية: Inorganic Chemistry, Chemical Sciences, Amycolatopsis, Bacterial Proteins, Catalytic Domain, Flavins, Mixed Function Oxygenases, Oxidation-Reduction, Baeyer-Villiger oxidation, flavin mononucleotide, mandelate oxidase, monooxygenase, oxidative decarboxylation, Biochemistry and Cell Biology, Computation Theory and Mathematics, Other Information and Computing Sciences, Biophysics, Biochemistry and cell biology, Medicinal and biomolecular chemistry
الوصف: Though reactive flavin-N5/C4α-oxide intermediates can be spectroscopically profiled for some flavin-assisted enzymatic reactions, their exact chemical configurations are hardly visualized. Structural systems biology and stable isotopic labelling techniques were exploited to correct this stereotypical view. Three transition-like complexes, the α-ketoacid…N5-FMNox complex (I), the FMNox -N5-aloxyl-C'α- -C4α+ zwitterion (II), and the FMN-N5-ethenol-N5-C4α-epoxide (III), were determined from mandelate oxidase (Hmo) or its mutant Y128F (monooxygenase) crystals soaked with monofluoropyruvate (a product mimic), establishing that N5 of FMNox an alternative reaction center can polarize to an ylide-like mesomer in the active site. In contrast, four distinct flavin-C4α-oxide adducts (IV-VII) from Y128F crystals soaked with selected substrates materialize C4α of FMN an intrinsic reaction center, witnessing oxidation, Baeyer-Villiger/peroxide-assisted decarboxylation, and epoxidation reactions. In conjunction with stopped-flow kinetics, the multifaceted flavin-dependent reaction continuum is physically dissected at molecular level for the first time.
وصف الملف: application/pdf
الوصول الحر: https://escholarship.org/uc/item/8xw3d695Test
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المؤلفون: Lin, Kuan-Hung, Lyu, Syue-Yi, Yeh, Hsien-Wei, Li, Yi-Shan, Hsu, Ning-Shian, Huang, Chun-Man, Wang, Yung-Lin, Shih, Hao-Wei, Wang, Zhe-Chong, Wu, Chang-Jer, Li, Tsung-Lin
المصدر: Protein science : a publication of the Protein Society, vol 29, iss 7
مصطلحات موضوعية: Biophysics, Computation Theory and Mathematics, Baeyer-Villiger oxidation, Mixed Function Oxygenases, flavin mononucleotide, Bacterial Proteins, Flavins, Catalytic Domain, oxidative decarboxylation, Biochemistry and Cell Biology, monooxygenase, Other Information and Computing Sciences, Oxidation-Reduction, Amycolatopsis, mandelate oxidase
الوصف: Though reactive flavin-N5/C4α-oxide intermediates can be spectroscopically profiled for some flavin-assisted enzymatic reactions, their exact chemical configurations are hardly visualized. Structural systems biology and stable isotopic labelling techniques were exploited to correct this stereotypical view. Three transition-like complexes, the α-ketoacid…N5-FMNox complex (I), the FMNox -N5-aloxyl-C'α- -C4α+ zwitterion (II), and the FMN-N5-ethenol-N5-C4α-epoxide (III), were determined from mandelate oxidase (Hmo) or its mutant Y128F (monooxygenase) crystals soaked with monofluoropyruvate (a product mimic), establishing that N5 of FMNox an alternative reaction center can polarize to an ylide-like mesomer in the active site. In contrast, four distinct flavin-C4α-oxide adducts (IV-VII) from Y128F crystals soaked with selected substrates materialize C4α of FMN an intrinsic reaction center, witnessing oxidation, Baeyer-Villiger/peroxide-assisted decarboxylation, and epoxidation reactions. In conjunction with stopped-flow kinetics, the multifaceted flavin-dependent reaction continuum is physically dissected at molecular level for the first time.
وصف الملف: application/pdf
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=od_______325::a85afd46ca1a2bb0e25b61a56b7e6e61Test
https://escholarship.org/uc/item/8xw3d695Test