pH Dependence of the polarographic limiting currents of α-keto acids

1961 ◽  
Vol 26 (1) ◽  
pp. 141-155 ◽  
Author(s):  
S. Ono ◽  
M. Takagi ◽  
T. Wasa
Keyword(s):  
2017 ◽  
Vol 121 (44) ◽  
pp. 8368-8379 ◽  
Author(s):  
Rebecca J. Rapf ◽  
Michael R. Dooley ◽  
Keaten Kappes ◽  
Russell J. Perkins ◽  
Veronica Vaida
Keyword(s):  

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

2019 ◽  
Author(s):  
Adrian Roitberg ◽  
Pancham Lal Gupta

<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>


1986 ◽  
Vol 51 (8) ◽  
pp. 1665-1670 ◽  
Author(s):  
Petr Kuzmič ◽  
Libuše Pavlíčková ◽  
Jiří Velek ◽  
Milan Souček
Keyword(s):  

Irradiation of 3,4-dimethoxy-1-nitrobenzene in the presence of butylamine leads to the formation of both possible photosubstitution products, i.e., 2-methoxy-4-nitro-N-butylaniline and 2-methoxy-5-nitro-N-butylaniline with the predominance of the latter. Regioselectivity of the reaction as measured by molar ratio of the two isomeric products varies with pH of the solution, ranging from 3 : 1 at pH 10 to 12. The results are discussed in view of possible use of 3,4-dimethoxy-1-nitrobenzene moiety as a lysine-directed photoaffinity probe.


1989 ◽  
Vol 54 (1) ◽  
pp. 64-69 ◽  
Author(s):  
Roland Meier ◽  
Gerhard Werner ◽  
Matthias Otto

Electrochemical oxidation of [V(IV)O(nta)(H2O)]- (H3nta nitrilotriacetic acid) was studied in aqueous solution by means of cyclic voltammetry, differential pulse polarography, and current sampled DC polarography on mercury as electrode material. In the pH-range under study (5.5-9.0) the corresponding V(V) complex is produced by one-electron oxidation of the parent V(IV) species. The oxidation product is stable within the time scale of cyclic voltammetry. The evaluation of the pH-dependence of the half-wave potentials leads to a pKa value for [V(IV)O(nta)(H2O)]- which is in a good agreement with previous determinations. The measured value for E1/2 is very close to the formal potential E0 calculated via the Nernst equation on the basis of known literature values for log Kox and log Kred, the complex stability constants for the oxidized and reduced form, respectively.


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