کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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59303 | 1419466 | 2011 | 4 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Ligninolytic Peroxidase-Like Activity of a Synthetic Metalloporphine Immobilized onto Mercapto-Grafted Crosslinked PVA Inspired by the Active Site of Cytochrome P450 Ligninolytic Peroxidase-Like Activity of a Synthetic Metalloporphine Immobilized onto Mercapto-Grafted Crosslinked PVA Inspired by the Active Site of Cytochrome P450](/preview/png/59303.png)
A synthetic metalloporphine was immobilized onto a PVA-based and mercapto-grafted solid support, emulating the active site of cytochrome P450. Its ligninolytic peroxidase-like catalytic activity was studied. The coordinated mercapto ligand significantly affected the catalytic features of the catalyst because the oxidation of lignin-model compounds was very slow by comparison with imidazole- and pyridine-coordinated immobilized metalloporphines. Conversely, the catalyst efficiently bleached several industrial dyes and thus demon-strated promising activity for this application. Based on this altered substrate specificity the oxygen-donor catalytic route seems to be more favorable than a single electron oxidation pathway.
FeTFPP was immobilized onto a solid support using a mercapto group as the ligand. The catalytic performance of the adduct was studied and we demonstrate that the presence of the -SH ligand dramatically changes its catalytic behavior.Figure optionsDownload as PowerPoint slide
Journal: Chinese Journal of Catalysis - Volume 32, Issues 11–12, November–December 2011, Pages 1663–1666