کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1935195 1050660 2008 4 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Kinetic evidence for rapid oxidation of (–)-epicatechin by human myeloperoxidase
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Kinetic evidence for rapid oxidation of (–)-epicatechin by human myeloperoxidase
چکیده انگلیسی

Apocynin has been reported to require dimerization by myeloperoxidase (MPO) to inhibit leukocyte NADPH oxidase. (–)-Epicatechin, a dietary flavan-3-ol, has been identified as a ‘prodrug’ of apocynin-like metabolites that inhibit endothelial NADPH oxidase activity and elevate the cellular level of nitric oxide. Since (–)-epicatechin has tentatively been identified as substrate of MPO, we studied the one-electron oxidation of (–)-epicatechin by MPO. By using multi-mixing stopped-flow technique, we demonstrate that (–)-epicatechin is one of the most efficient electron donors for heme peroxidases investigated so far. Second order rate constants for the (–)-epicatechin-mediated conversion of MPO-compound I to compound II and compound II to resting enzyme were estimated to be 1.9 × 107 and 4.5 × 106 M−1 s−1, respectively (pH 7, 25 °C). The data indicate that (–)-epicatechin is capable of undergoing fast MPO-mediated one-electron oxidation.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 371, Issue 4, 11 July 2008, Pages 810–813
نویسندگان
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