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|Title:||Analysis of spin configuration and catalytic activity of mutated horse cytochrome c immobilized in mesoporoous material|
|Citation:||Pure and Applied Chemistry International Conference 2011);102|
|Abstract:||Cytochrome c, an iron containing heme protein, can act as a biocatalyst for the decomposition of organic compounds in the present of hydrogen peroxide (H2O2); that is “peroxidase-like activity”. It has been demonstrated that the activity of cytochrome c is enhanced when immobilized in confined environments compared to the native folded state. In this work, horse cytochrome c is immobilized in the nanochannels of a mesoporous material, i.e., MCM-41. The peroxidase-like activity of cytochrome c in MCM-41 is about three times higher than that in buffer solution. The cytochrome c in MCM-41 is the one of the most important factors enhancing peroxidase activity in the accessibility of the iron site for H2O2 binding. Accordingly, the spin configuration of the heme iron is determined by Electron Spin Resonance (ESR). The native cytochrome c is composed of low-spin Fe(III) state. Previous study has shown that cytochrome c in MCM-41 contains higher portion of high-spin Fe(III), which is related to the higher activity. The structural changes of ytochrome c caused by the enclosed surroundings; therefore, facilitate the reaction of H2O2 at the heme iron site. To gain the picture of local structures in different part of cytochrome c, site-directed mutagenesis is performed at G34C (coilregion) and I95C (helix structure). The analysis of Fe(III) spin states combined with the peroxidase-like activity of the mutants in solution and MCM-41 will elucidate how the conformations of the protein at position G34C and I95C affect the activity of immobilized cytochrome c systems.|
|Appears in Collections:||Chemistry: International Proceedings|
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