Effect of solvent type on the formation rate of benzyl cation intermediate in acidolysis of lignin

The purpose of this study was to examine how the type of solvent among aqueous 1,4-dioxane, tetrahydrofuran, ethanol, iso-propyl alcohol, or ethylene glycol and its content (mol%) affect the formation rate of benzyl cation intermediate (BC) in the acidolysis of lignin, using a simple model compound, 1,2-dimethoxy-4-methoxymethylbenzene. Because the BC forms from the model compound via two steps, i.e., protonation of the benzyl methoxymethyl group as the pre-equilibrium step and liberation of the methanol as the rate-determining step, the observed variation of the formation rate with type of solvent and solvent content originates from the effects on both steps undistinguishably. The formation rate of BC decreased with increasing mol% of any of the organic solvents for a range of relatively low mol%, but increased with it for relatively high mol%. The formation rate varied more in the ether than in the alcohol systems. These results seem to be regulated by the effect of changing the mol% on the pre-equilibrium step, i.e., on the proton activity, rather than on the rate-determining step. Two reaction products, 4-alkoxymethyl-1,2-dimethoxybenzene and 4-hydroxymethyl-1,2-dimethoxybenzene, exclusively formed in the aqueous alcohol systems. The former compound was confirmed to be thermodynamically more stable and kinetically the more favorable product.

Molecular mechanism of glycolytic flux control intrinsic to human phosphoglycerate kinase

Glycolysis plays a fundamental role in energy production and metabolic homeostasis. The intracellular [adenosine triphosphate]/[adenosine diphosphate] ([ATP]/[ADP]) ratio controls glycolytic flux; however, the regulatory mechanism underlying reactions catalyzed by individual glycolytic enzymes enabling flux adaptation remains incompletely understood. Phosphoglycerate kinase (PGK) catalyzes the reversible phosphotransfer reaction, which directly produces ATP in a near-equilibrium step of glycolysis. Despite extensive studies on the transcriptional regulation of PGK expression, the mechanism in response to changes in the [ATP]/[ADP] ratio remains obscure. Here, we report a protein-level regulation of human PGK (hPGK) by utilizing the switching ligand-binding cooperativities between adenine nucleotides and 3-phosphoglycerate (3PG). This was revealed by nuclear magnetic resonance (NMR) spectroscopy at physiological salt concentrations. MgADP and 3PG bind to hPGK with negative cooperativity, whereas MgAMPPNP (a nonhydrolyzable ATP analog) and 3PG bind to hPGK with positive cooperativity. These opposite cooperativities enable a shift between different ligand-bound states depending on the intracellular [ATP]/[ADP] ratio. Based on these findings, we present an atomic-scale description of the reaction scheme for hPGK under physiological conditions. Our results indicate that hPGK intrinsically modulates its function via ligand-binding cooperativities that are finely tuned to respond to changes in the [ATP]/[ADP] ratio. The alteration of ligand-binding cooperativities could be one of the self-regulatory mechanisms for enzymes in bidirectional pathways, which enables rapid adaptation to changes in the intracellular environment.

Monitoring of the Pre-Equilibrium Step in the Alkyne Hydration Reaction Catalyzed by Au(III) Complexes: A Computational Study Based on Experimental Evidences

The coordination ability of the [(ppy)Au(IPr)]2+ fragment [ppy = 2-phenylpyridine, IPr = 1,3-bis(2,6-di-isopropylphenyl)-imidazol-2-ylidene] towards different anionic and neutral X ligands (X = Cl−, BF4−, OTf−, H2O, 2-butyne, 3-hexyne) commonly involved in the crucial pre-equilibrium step of the alkyne hydration reaction is computationally investigated to shed light on unexpected experimental observations on its catalytic activity. Experiment reveals that BF4− and OTf− have very similar coordination ability towards [(ppy)Au(IPr)]2+ and slightly less than water, whereas the alkyne complex could not be observed in solution at least at the NMR sensitivity. Due to the steric hindrance/dispersion interaction balance between X and IPr, the [(ppy)Au(IPr)]2+ fragment is computationally found to be much less selective than a model [(ppy)Au(NHC)]2+ (NHC = 1,3-dimethylimidazol-2-ylidene) fragment towards the different ligands, in particular OTf− and BF4−, in agreement with experiment. Effect of the ancillary ligand substitution demonstrates that the coordination ability of Au(III) is quantitatively strongly affected by the nature of the ligands (even more than the net charge of the complex) and that all the investigated gold fragments coordinate to alkynes more strongly than H2O. Remarkably, a stabilization of the water-coordinating species with respect to the alkyne-coordinating one can only be achieved within a microsolvation model, which reconciles theory with experiment. All the results reported here suggest that both the Au(III) fragment coordination ability and its proper computational modelling in the experimental conditions are fundamental issues for the design of efficient catalysts.

Hydration of alkynes catalyzed by [Au(X)(L)(ppy)]X in the green solvent γ-valerolactone under acid-free conditions: the importance of the pre-equilibrium step

Stable and robust [Au(H2O)(NHC)(ppy)](X)2 successfully catalyses the hydration of alkynes in GVL, under acid-free conditions. DFT calculation and NMR measurements suggest that pre-equilibrium is the key step of the whole process.

Mn(II) Catalyzed Oxidation of Atenolol by Cerium(IV) in Aqueous Sulfuric Acid Medium: A Spectrophotometer Aided Kinetic, Mechanistic and Thermodynamic Study

The kinetics and mechanism of manganese(II) catalyzed oxidation of atenolol by cerium(IV) sulfate in aqueous H2SO4at a constant ionic strength of 0.50 mol dm-3was studied spectrophotometrically. The reaction showed first order kinetics in cerium(IV) whereas fractional order in both manganese(II) and atenolol. Addition of products showed no effect on the rate of the reaction. The main product, 2-(4-(2-hydroxy-3-oxopropoxy)phenyl)acetamide, was identified with the aid of IR and mass spectral data. Stoichiometry with respect to the drug substrate and reagent was established as 2:1. Added H2SO4, SO42−and HSO4−showed negligible effect on the rate of the reaction. HCe(SO4)3−was found to be the predominant reactive species under the specified experimental conditions. The rate constants (k), catalytic constant (kc) and equilibrium constant (K6) for the proposed mechanism were determined. The kinetic and thermodynamic activation parameters were computed for both the slow rate determining step and complex forming equilibrium step.

Kinetics and Mechanism of 2,2′-bipyridine Catalysed Chromium(VI) Oxidation of Dimethyl Sulfoxide in the Presence and Absence of Surfactants†

In the 2,2′-bipyridine (bipy) catalysed CrVI oxidation of dimethyl sulfoxide (DMSO) to dimethyl sulfone, the CrVI–bipy complex formed at the pre - equilibrium step undergoes a nucleophilic attack by the S or O of DMSO to form a positively charged reactive intermediate. This intermediate experiences an oxygen transfer or a ligand coupling to give the products. The anionic surfactant (SDS) accelerates the process while the cationic surfactant (CPC) retards the reaction.

Mechanism of Oxidation of L-Histidine by Heptavalent Manganese in Alkaline Medium

The kinetics of oxidation of L-histidine by manganese(VII) in aqueous alkaline medium at a constant ionic strength of 0.05 mol dm-3was studied spectrophotometrically. The reaction between permanganate and L-histidine in alkaline medium exhibits 2:1 stoichiometry (KMnO4: L-histidine). The reaction is of first order in [KMnO4], less than unit order in [L-histidine] and [alkali]. Decrease in the dielectric constant of the medium decreases the rate of reaction. Effect of added products and ionic strength of the reaction medium have been investigated. The main products were identified by spot test and I.R. A mechanism involving the free radical has been proposed. In composite equilibrium step L-histidine binds to MnO4-species to form a complex(C). The reaction constants involved in the different steps of mechanism are evaluated. The activation parameters with respect to slow step of the mechanism are computed and discussed and thermodynamic quantities are also determined.