Role of Hydroxyl Group in the Inhibitive Action of Benzoic Acid Toward Corrosion of Aluminum in Nitric Acid

CORROSION ◽  
1999 ◽  
Vol 55 (10) ◽  
pp. 937-941 ◽  
Author(s):  
P. N. S. Yadav ◽  
A. K. Singh ◽  
R. Wadhwani
2021 ◽  
pp. 130581
Author(s):  
Shuai Shao ◽  
Gaobo Wang ◽  
Zhimin Gong ◽  
Mengjie Wang ◽  
Jianhua Hu ◽  
...  
Keyword(s):  

ChemSusChem ◽  
2014 ◽  
Vol 8 (3) ◽  
pp. 466-472 ◽  
Author(s):  
Sankaranarayanapillai Shylesh ◽  
David Hanna ◽  
Joseph Gomes ◽  
Christian G. Canlas ◽  
Martin Head-Gordon ◽  
...  

2021 ◽  
Author(s):  
Chih-Wei Huang ◽  
Chi-Ching Hwang ◽  
Yung-Lung Chang ◽  
Jen-Tzu Liu ◽  
Sheng-Peng Wu ◽  
...  

4-Hydroxylphenylpyruvate dioxygenase (HPPD) catalyzes the conversion of 4-hydroxylphenylpyruvate (HPP) to homogentisate, the important step for tyrosine catabolism. Comparison of the structure of human HPPD with the substrate-bound structure of A. thaliana HPPD revealed notably different orientations of the C-terminal helix. This helix performed as a closed conformation in human enzyme. Simulation revealed a different substrate-binding mode in which the carboxyl group of HPP interacted by a H-bond network formed by Gln334, Glu349 (the metal-binding ligand), and Asn363 (in the C-terminal helix). The 4-hydroxyl group of HPP interacted with Gln251 and Gln265. The relative activity and substrate-binding affinity were preserved for the Q334A mutant, implying the alternative role of Asn363 for HPP binding and catalysis. The reduction in kcat/Km of the Asn363 mutants confirmed the critical role in catalysis. Compared to the N363A mutant, the dramatic reduction in the Kd and thermal stability of the N363D mutant implies the side-chain effect in the hinge region rotation of the C-terminal helix. The activity and binding affinity were not recovered by double mutation; however, the 4-hydroxyphenylacetate intermediate formation by the uncoupled reaction of Q334N/N363Q and Q334A/N363D mutants indicated the importance of the H-bond network in the electrophilic reaction. These results highlight the functional role of the H-bond network in a closed conformation of the C-terminal helix to stabilize the bound substrate. The extremely low activity and reduction in Q251E’s Kd suggest that interaction coupled with the H-bond network is crucial to locate the substrate for nucleophilic reaction.


2012 ◽  
Vol 296 (1) ◽  
pp. 27-30 ◽  
Author(s):  
Bruce J. Mincher ◽  
Martin Precek ◽  
Stephen P. Mezyk ◽  
Leigh R. Martin ◽  
Alena Paulenova
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Author(s):  
Xin Mi ◽  
Shuangxi Zhou ◽  
Ziming Zhou ◽  
Mohammadtaghi Vakili ◽  
Yue Qi ◽  
...  

1967 ◽  
Vol 10 (5) ◽  
pp. 908-912 ◽  
Author(s):  
Alexander. Bloch ◽  
Morris J. Robins ◽  
James R. McCarthy

Author(s):  
J. R. Lindsay Smith ◽  
D. I. Richards ◽  
C. B. Thomas ◽  
M. Whittaker
Keyword(s):  

2016 ◽  
Vol 157 ◽  
pp. 791-797 ◽  
Author(s):  
Riccardo Paolini ◽  
Mohamad Sleiman ◽  
MariaPia Pedeferri ◽  
Maria Vittoria Diamanti
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