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C-N bond formation is regarded as a very useful and fundamental reaction, which is important for the synthesis of nitrogen-containing molecules in both organic and pharmaceutical chemistry. Noble metal and homogeneous catalysts have been used for C-N bond formation frequently, however, there are still some problems for these catalysts such as high cost, serious pollution and low atom economy. Herein the low-toxic and cheaper iron complex was loaded on CNTs and the heterogenous single-atom catalyst (SAC) named Fe-N x /CNTs was prepared. We applied this SAC to the synthesis of C-N bonds for the first time. It was found that Fe-N x /CNTs was an efficient catalyst for the synthesis of C-N bonds from aromatic amines and ketones. The catalytic performance is markedly excellent with the yield up to 96%, 6-fold higher than that of noble metal catalysts such as AuCl 3 /CNTs and RhCl 3 /CNTs. It was suitable for up to 13 aromatic amine substrates with no additives and 17 enaminones were obtained. By using high-angle annular darkfield scanning transmission electron microscopy (HAADF-STEM) in combination with X-ray adsorption spectroscopy (XAS), we have observed iron species of Fe-N x /CNTs were in good dispersion as single atoms and Fe-N x might be the catalytic active site. This Fe-N x /CNTs catalyst has potential industrial application for its seven runs without any significant loss of activity.
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Name: Chemistry (Weinheim an der Bergstrasse, Germany)
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A class of iron-sulfur proteins that contains one iron coordinated to the sulfur atom of four cysteine residues. (McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
Iron or iron compounds used in foods or as food. Dietary iron is important in oxygen transport and the synthesis of the iron-porphyrin proteins hemoglobin, myoglobin, cytochromes, and cytochrome oxidase. Insufficient amounts of dietary iron can lead to iron-deficiency anemia.
A multifunctional iron-sulfur protein that is both an iron regulatory protein and cytoplasmic form of aconitate hydratase. It binds to iron regulatory elements found on mRNAs involved in iron metabolism and regulates their translation. Its rate of degradation is increased in the presence of IRON.
A multifunctional iron-sulfur protein that is both an iron regulatory protein and cytoplasmic form of aconitate hydratase. It binds to iron regulatory elements found on mRNAs involved in iron metabolism and regulates their translation. Its RNA binding ability and its aconitate hydrolase activity are dependent upon availability of IRON.
Hemeproteins whose characteristic mode of action involves transfer of reducing equivalents which are associated with a reversible change in oxidation state of the prosthetic group. Formally, this redox change involves a single-electron, reversible equilibrium between the Fe(II) and Fe(III) states of the central iron atom (From Enzyme Nomenclature, 1992, p539). The various cytochrome subclasses are organized by the type of HEME and by the wavelength range of their reduced alpha-absorption bands.
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