pH Dependence of the Belousov−Zhabotinsky Reaction in Water-in-Oil Reverse Microemulsion of AOT in Octane

1996 ◽  
Vol 100 (25) ◽  
pp. 10609-10614 ◽  
Author(s):  
Vladimir K. Vanag ◽  
Ichiro Hanazaki
Keyword(s):  
Ph Dependence ◽  
Reverse Microemulsion ◽  
Belousov Zhabotinsky Reaction ◽  
Reaction In Water

Modulation of volume fraction results in different kinetic effects in Belousov–Zhabotinsky reaction confined in AOT-reverse microemulsion

2011 ◽  
Vol 134 (9) ◽  
pp. 094512 ◽  
Author(s):  
Eva Villar Álvarez ◽  
Jorge Carballido-Landeira ◽  
Jacobo Guiu-Souto ◽  
Pablo Taboada ◽  
Alberto P. Muñuzuri
Keyword(s):  
Volume Fraction ◽  
Reverse Microemulsion ◽  
Kinetic Effects ◽  
Belousov Zhabotinsky Reaction

Self-association of insulin. Its pH dependence and effect of plasma

Diabetes ◽  
1987 ◽  
Vol 36 (3) ◽  
pp. 261-264 ◽  
Author(s):  
E. Helmerhorst ◽  
G. B. Stokes
Keyword(s):  
Ph Dependence ◽  
Self Association

Rationalizing the pH-Activity Response for Escherichia Coli’s Glycinamide Ribonucleotidetransformylase Through Computational Methods

2019 ◽  
Author(s):  
Adrian Roitberg ◽  
Pancham Lal Gupta
Keyword(s):  
Transfer Reaction ◽  
Catalytic Mechanism ◽  
Ph Dependence ◽  
Ph Effects ◽  
Dependent Manner ◽  
E Coli ◽  
Gar Tfase ◽  
Activity Curve ◽  
Ph Dependent ◽  
Formyl Transfer

<div>Human Glycinamide ribonucleotide transformylase (GAR Tfase), a regulatory enzyme in the de novo purine biosynthesis pathway, has been established as an anti-cancer target. GAR Tfase catalyzes the formyl transfer reaction from the folate cofactor to the GAR ligand. In the present work, we study E. coli GAR Tfase, which has high sequence similarity with the human GAR Tfase with most functional residues conserved. E. coli GAR Tfase exhibits structural changes and the binding of ligands that varies with pH which leads to change the rate of the formyl transfer reaction in a pH-dependent manner. Thus, the inclusion of pH becomes essential for the study of its catalytic mechanism. Experimentally, the pH-dependence of the kinetic parameter kcat is measured to evaluate the pH-range of enzymatic activity. However, insufficient information about residues governing the pH-effects on the catalytic activity leads to ambiguous assignments of the general acid and base catalysts and consequently its catalytic mechanism. In the present work, we use pH-replica exchange molecular dynamics (pH-REMD) simulations to study the effects of pH on E. coli GAR Tfase enzyme. We identify the titratable residues governing the pH-dependent conformational changes in the system. Furthermore, we filter out the protonation states which are essential in maintaining the structural integrity, keeping the ligands bound and assisting the catalysis. We reproduce the experimental pH-activity curve by computing the population of key protonation states. Moreover, we provide a detailed description of residues governing the acidic and basic limbs of the pH-activity curve.</div>

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