The Chemistry of High Valent Vanadium Oxo Species Interacting with Trisbezenethiolatosilane Ligands

碩士 === 國立成功大學 === 化學系碩博士班 === 92 ===   My research has been interested in studying vanadium thiolate chemistry due to its biological significance. Particularly, to understand the protein-tyrosine phosphatase (PTP) which is inhibited by vanadate through the interaction with the Cys residue in the en...

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Main Authors: Gui-Shih Huang, 黃桂施
Other Authors: Hua-Fen Hsu
Format: Others
Language:zh-TW
Published: 2004
Online Access:http://ndltd.ncl.edu.tw/handle/778eyc
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spelling ndltd-TW-092NCKU50650402019-05-15T20:21:37Z http://ndltd.ncl.edu.tw/handle/778eyc The Chemistry of High Valent Vanadium Oxo Species Interacting with Trisbezenethiolatosilane Ligands 高價釩與多硫配位基的反應 Gui-Shih Huang 黃桂施 碩士 國立成功大學 化學系碩博士班 92   My research has been interested in studying vanadium thiolate chemistry due to its biological significance. Particularly, to understand the protein-tyrosine phosphatase (PTP) which is inhibited by vanadate through the interaction with the Cys residue in the enzyme, I focus my research on the basic chemistry of VO3+ species interacting with thiolato ligands. In the reaction of VO3+ with trisbezenethiolatosilane ligand system, PhSiS3, SiS3 and SiS3’,1 we obtained unexpected divanadium(IV) dioxo complexes, I, II, and III, showing in the following scheme. The formation of compounds I, II, and III indicates that the Si-H/Si-C bonds are cleaved during the reaction.   In addition, in order to understand the role of the heterometallic site in the cofactor of nitrogenase, I develop a novel ligand, S3N (IV), which might provide the metal complexes containing the coordination environment similar to that of the heterometallic site of the enzyme. Hua-Fen Hsu 許鏵芬 2004 學位論文 ; thesis 93 zh-TW
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description 碩士 === 國立成功大學 === 化學系碩博士班 === 92 ===   My research has been interested in studying vanadium thiolate chemistry due to its biological significance. Particularly, to understand the protein-tyrosine phosphatase (PTP) which is inhibited by vanadate through the interaction with the Cys residue in the enzyme, I focus my research on the basic chemistry of VO3+ species interacting with thiolato ligands. In the reaction of VO3+ with trisbezenethiolatosilane ligand system, PhSiS3, SiS3 and SiS3’,1 we obtained unexpected divanadium(IV) dioxo complexes, I, II, and III, showing in the following scheme. The formation of compounds I, II, and III indicates that the Si-H/Si-C bonds are cleaved during the reaction.   In addition, in order to understand the role of the heterometallic site in the cofactor of nitrogenase, I develop a novel ligand, S3N (IV), which might provide the metal complexes containing the coordination environment similar to that of the heterometallic site of the enzyme.
author2 Hua-Fen Hsu
author_facet Hua-Fen Hsu
Gui-Shih Huang
黃桂施
author Gui-Shih Huang
黃桂施
spellingShingle Gui-Shih Huang
黃桂施
The Chemistry of High Valent Vanadium Oxo Species Interacting with Trisbezenethiolatosilane Ligands
author_sort Gui-Shih Huang
title The Chemistry of High Valent Vanadium Oxo Species Interacting with Trisbezenethiolatosilane Ligands
title_short The Chemistry of High Valent Vanadium Oxo Species Interacting with Trisbezenethiolatosilane Ligands
title_full The Chemistry of High Valent Vanadium Oxo Species Interacting with Trisbezenethiolatosilane Ligands
title_fullStr The Chemistry of High Valent Vanadium Oxo Species Interacting with Trisbezenethiolatosilane Ligands
title_full_unstemmed The Chemistry of High Valent Vanadium Oxo Species Interacting with Trisbezenethiolatosilane Ligands
title_sort chemistry of high valent vanadium oxo species interacting with trisbezenethiolatosilane ligands
publishDate 2004
url http://ndltd.ncl.edu.tw/handle/778eyc
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