Effect of electron-donating substituent groups on aromatic ring on photoluminescence properties of complexes of benzoic acid-functionalized polysulfone with Eu(iii) ions

2015 ◽  
Vol 17 (38) ◽  
pp. 25322-25332 ◽  
Author(s):  
Baojiao Gao ◽  
Lulu Chen ◽  
Tao Chen

By molecular design and via polymer reactions, methoxybenzoic acid (MOBA) and hydroxybenzoic acid (HBA) were bonded onto the side chains of polysulfone (PSF) for preparing two benzoic acid-functionalized PSFs, PSF-MOBA and PSF-HBA, respectively.

2008 ◽  
Vol 3 (3) ◽  
pp. 1934578X0800300
Author(s):  
Juan Manuel Amaro-Luis ◽  
Sonia Koteich-Khatib ◽  
Freddy Carrillo-Rodríguez ◽  
Alí Bahsas

A new prenylated benzoic acid derivative, named myrsicorianol (1), was isolated from the fruits of Myrsine coriacea and its structure was determined by spectral analysis, including 1D- and 2D-NMR experiments. Myrsinoic acid A and a mixture of the p-benzoquinones, embelin, rapanone and 2,5-dihydroxy-3-pentadecyl-1,4-benzoquinone (homorapanone) were also obtained from the fruits, whilst the bark afforded myrsinoic acid A, myrsinoic acid B, 3-(3′,7′-dimethyl-2′,6′-octadienyl)-4-hydroxybenzoic acid and 3-(3′,7′-dimethyl-2′,6′-octadienyl)-4-methoxybenzoic acid.


1967 ◽  
Vol 13 (7) ◽  
pp. 761-769 ◽  
Author(s):  
E. R. Blakley

A strain of Pseudomonas previously used to study the oxidative degradation of phenylacetic acid and phenylpropionic acid has been used to study the degradation of p-hydroxybenzoic acid, L-tyrosine, L-phenylalanine, phenylbutyric acid, and phenylvaleric acid. p-Hydroxybenzoic acid was converted to 3, 4-dihydroxy-benzoic acid and the aromatic ring was cleaved between carbons 3 and 4. Previous results showed that cleavage of 3, 4-dihydroxyphenylacetic acid occurred between carbons 2 and 3. Phenylalanine and tyrosine were metabolized by the homogentisic acid pathway. These results, together with results of previous work, suggest that the pathway used for the degradation of aromatic compounds by this organism varies with the nature of the side chain. The metabolism of aromatic compounds with side chains longer than three carbons appears to involve oxidative shortening of the side chain prior to cleavage of the aromatic ring.


Soft Matter ◽  
2021 ◽  
Author(s):  
Zhiqiang Zhao ◽  
Zheng Bian ◽  
Yu Chen ◽  
Chuanqing Kang ◽  
Lianxun Gao ◽  
...  

Chiral oligo(methylene-p-phenyleneethynylene)s can form vesicular assemblies no matter whether side chains and solvents are hydrophilic or hydrophobic. The self-assembly processes are highly independent of molecular design and chemical environments.


Author(s):  
G. Beaven ◽  
A. Bowyer ◽  
P. Erskine ◽  
S. P. Wood ◽  
A. McCoy ◽  
...  

The enzyme 2,4′-dihydroxyacetophenone dioxygenase (or DAD) catalyses the conversion of 2,4′-dihydroxyacetophenone to 4-hydroxybenzoic acid and formic acid with the incorporation of molecular oxygen. Whilst the vast majority of dioxygenases cleave within the aromatic ring of the substrate, DAD is very unusual in that it is involved in C—C bond cleavage in a substituent of the aromatic ring. There is evidence that the enzyme is a homotetramer of 20.3 kDa subunits each containing nonhaem iron and its sequence suggests that it belongs to the cupin family of dioxygenases. By the use of limited chymotrypsinolysis, the DAD enzyme fromAlcaligenessp. 4HAP has been crystallized in a form that diffracts synchrotron radiation to a resolution of 2.2 Å.


1976 ◽  
Vol 31 (11-12) ◽  
pp. 693-699 ◽  
Author(s):  
W. Löffelhardt ◽  
H. Kindl

Abstract Membrane-Bound Enzyme Complexes, Anacystis nidulans, Thylakoids, Benzoate Synthase The photosynthetic procaryote Anacystis nidulans converts L-phenylalanine and L-tyrosine into benzoic acid and p-hydroxybenzoic acid, respectively. Results obtained with thylakoid fractions support the hypothesis that the reaction sequence is catalyzed by thylakoid-bound enzyme complexes consisting of phenylalanine ammonia-lyase and benzoate synthase or tyrosine ammonia-lyase and p-hydroxybenzoate synthase, respectively. Both complexes do not accept phenylacetic acids as substrates, and cinnamic acids only at a small extent. These properties suggest a striking similarity to a benzoic acid-synthesizing enzyme system from higher plants which is situated at the thylakoid membrane of chloroplasts. The respective complexes of Dunaliella marina and Porphyridium sp. were included in this comparison.


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