2次元化学抵抗性高伝導性共振性有機フレームワーク
Zheng Meng1, Robert M Stolz1, Katherine A Mirica1
1Department of Chemistry, Burke Laboratory , Dartmouth College , Hanover , New Hampshire 03755 , United States.
Journal of the American Chemical Society
|June 27, 2019
まとめ
研究者は,新しい導電性2D共電性有機フレームワーク (COF) 材料,COF-DC-8を合成しました. この材料は 優れたガスの検知能力を持ち 10億分の1のレベルでのガスを検知します
科学分野:
- 材料科学
- ナノテクノロジー
- 化学について
背景:
- 二次元 (2D) 材料はユニークな電子特性を提供します.
- 協和有機フレームワーク (COF) は,調節可能な構造を持つ結晶性多孔ポリマーである.
- 先進的な電子アプリケーションでは,本質的に導電性COFの開発が不可欠です.
研究 の 目的:
- 本質的に導電性の2D COFを合成する.
- 合成されたCOFのガス感知性能を調査する.
- COFのガス感知反応の背後にあるメカニズムを解明する.
主な方法:
- ニッケル (II) オクタアミノフタロシアンとピレン-4,5,9,10-テトラオンの間の芳香無効反応.
- ヨウ素 (I2) ドーピング前後の電気伝導度測定
- ガス検出のための化学抵抗装置の製造.
- 電子構造の計算
- 電子パラマグネティック共振 (EPR) とX線光電子スペクトロスコピー (XPS) の分析
主要な成果:
- 本質的に伝導性のある新しい2D COF,COF-DC-8が成功して合成されました.
- COF-DC-8は,I2ドーピングで3桁の大きさで増加した2.51 × 10−3 S/mの固有の散布伝導性を示した.
- この材料は,各種のガス (NH3,H2S,NO,NO2) を,パーツ・パー・ビリオン (ppb) レベルで検出するための高い感度と選択性を示した.
- 電子計算では,伝導性に潜在的に寄与するアニソトロピックバンド構造を示した.
- 研究では,分析物質とニッケルフタロシアニンの間の電荷移転相互作用が検出メカニズムに起因すると示唆されています.
結論:
- 合成されたCOF-DC-8は,ガスセンシングアプリケーションのための有望な伝導材料です.
- 材料の伝導性とガス感知性能はドーピングによって著しく向上します.
- ニッケルフタロシアニンは,ガス検出のための電荷移転機構において重要な役割を果たします.
関連する概念動画
02:18Network Covalent Solids
16.1K
Network covalent solids contain a three-dimensional network of covalently bonded atoms as found in the crystal structures of nonmetals like diamond, graphite, silicon, and some covalent compounds, such as silicon dioxide (sand) and silicon carbide (carborundum, the abrasive on sandpaper). Many minerals have networks of covalent bonds.
To break or to melt a covalent network solid, covalent bonds must be broken. Because covalent bonds are relatively strong, covalent network solids are typically...
To break or to melt a covalent network solid, covalent bonds must be broken. Because covalent bonds are relatively strong, covalent network solids are typically...
16.1K
02:18Intrinsically Disordered Proteins
19.2K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
19.2K
02:18Intrinsically Disordered Proteins
2.8K
2.8K
01:29Covalent Bonds
160.5K
Overview
160.5K
01:08Covalent Bonds
10.1K
Overview
When two atoms share electrons to complete their valence shells, they create a covalent bond. An atom's electronegativity—the force with which shared electrons are pulled towards an atom—determines how the electrons are shared. Molecules formed with covalent bonds can be either polar or nonpolar. Atoms with similar electronegativities form nonpolar covalent bonds; the electrons are shared equally. Atoms with different electronegativities share electrons unequally,...
When two atoms share electrons to complete their valence shells, they create a covalent bond. An atom's electronegativity—the force with which shared electrons are pulled towards an atom—determines how the electrons are shared. Molecules formed with covalent bonds can be either polar or nonpolar. Atoms with similar electronegativities form nonpolar covalent bonds; the electrons are shared equally. Atoms with different electronegativities share electrons unequally,...
10.1K
02:04Covalently Linked Protein Regulators
8.8K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
These groups modify specific amino acids in a protein....
8.8K