Catalytic mechanisms of oxygen-containing groups over vanadium active sites in an Al-MCM-41 framework for production of 2,5-diformylfuran from 5-hydroxymethylfurfural

2020 ◽  
Vol 10 (1) ◽  
pp. 278-290 ◽  
Author(s):  
Li-Juan Liu ◽  
Zhao-Meng Wang ◽  
Ya-Jing Lyu ◽  
Jin-Feng Zhang ◽  
Zhou Huang ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Active Site ◽  
Active Sites ◽  
Hydroxyl Group ◽  
Catalytic Mechanisms ◽  
Mcm 41

In the V-doped Al-MCM-41 framework, the [V-1] active site with a hydroxyl group displays better catalytic activity than the [V-0] active site without a hydroxyl group toward the oxidation of 5-hydroxymethylfurfural to 2,5-diformylfuran.

The design and catalytic performance of molybdenum active sites on an MCM-41 framework for the aerobic oxidation of 5-hydroxymethylfurfural to 2,5-diformylfuran

2019 ◽  
Vol 9 (3) ◽  
pp. 811-821 ◽  
Author(s):  
Zhao-Meng Wang ◽  
Li-Juan Liu ◽  
Bo Xiang ◽  
Yue Wang ◽  
Ya-Jing Lyu ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Active Sites ◽  
Aerobic Oxidation ◽  
Catalytic Performance ◽  
Mcm 41

The catalytic activity decreases as –(SiO)3Mo(OH)(O) > –(SiO)2Mo(O)2 > –(O)4–MoO.

On the role of lysine in the active site Ser-X-X-Lys region of penicillin-recognizing enzymes

2010 ◽  
Vol 88 (1) ◽  
pp. 1-4
Author(s):  
Saul Wolfe ◽  
Kiyull Yang
Keyword(s):  
Active Site ◽  
Active Sites ◽  
Density Functional ◽  
Basis Set ◽  
Penicillin G ◽  
Hydroxyl Group ◽  
Functional Theory ◽  
One Step ◽  
Optimized Geometries

Using Autodock, docking of penicillin G to the crystal structures of penicillin-recognizing enzymes leads to an alignment in the active site Ser-X-X-Lys region consisting of the serine hydroxyl group, the terminal amino group of lysine, a second hydroxyl group, and the N–C=O of the β-lactam. This alignment is consistent with the notion that acylation of the serine hydroxyl group proceeds by a one-step cooperative mechanism in which C–O bond formation and proton transfer to the β-lactam nitrogen take place through a heteroatom bridge. For the cooperative ring opening of penam by two molecules of methanol and one molecule of methylamine or one molecule of water, density functional theory with the B3LYP DFT gradient-corrected functional and the 6–31G(d) basis set reproduces the alignment seen in the docked structures. Methylamine lowers the barrier calculated at MP2/6–31G(d) from the DFT-optimized geometries by 3 kcal/mol; water increases the barrier by 4 kcal/mol. The function of the conserved lysine in the active sites of penicillin-recognizing enzymes is therefore to catalyze the formation of an acyl enzyme by a cooperative mechanism.

scholarly journals The Role of Glutathione in the Isomerization of Δ5-Androstene- 3,17-dione Catalyzed by Human Glutathione Transferase A1-1

2001 ◽  
Vol 276 (15) ◽  
pp. 11698-11704 ◽  
Author(s):  
Pär L. Pettersson ◽  
Bengt Mannervik
Keyword(s):  
Active Site ◽  
Active Sites ◽  
Catalytic Mechanism ◽  
Glutathione Transferase ◽  
Ph Dependence ◽  
Enzymatic Catalysis ◽  
Catalytic Efficiency ◽  
Protonated Form ◽  
Hydroxyl Group ◽  
Isomerization Reaction

Human glutathione transferase (GST) A1-1 efficiently catalyzes the isomerization of Δ5-androstene-3,17-dione (AD) into Δ4-androstene-3,17-dione. High activity requires glutathione, but enzymatic catalysis occurs also in the absence of this cofactor. Glutathione alone shows a limited catalytic effect.S-Alkylglutathione derivatives do not promote the reaction, and the pH dependence of the isomerization indicates that the glutathione thiolate serves as a base in the catalytic mechanism. Mutation of the active-site Tyr9into Phe significantly decreases the steady-state kinetic parameters, alters their pH dependence, and increases the pKavalue of the enzyme-bound glutathione thiol. Thus, Tyr9promotes the reaction via its phenolic hydroxyl group in protonated form. GST A2-2 has a catalytic efficiency with AD 100-fold lower than the homologous GST A1-1. Another Alpha class enzyme, GST A4-4, is 1000-fold less active than GST A1-1. The Y9F mutant of GST A1-1 is more efficient than GST A2-2 and GST A4-4, both having a glutathione cofactor and an active-site Tyr9residue. The active sites of GST A2-2 and GST A1-1 differ by only four amino acid residues, suggesting that proper orientation of AD in relation to the thiolate of glutathione is crucial for high catalytic efficiency in the isomerization reaction. The GST A1-1-catalyzed steroid isomerization provides a complement to the previously described isomerase activity of 3β-hydroxysteroid dehydrogenase.

Structure of Hydrogenase in Biohydrogen Production Anaerobic Bacteria

2011 ◽  
pp. 251-258 ◽  
Author(s):  
Ming Du ◽  
Lu Zhang
Keyword(s):  
Active Site ◽  
Active Sites ◽  
Catalytic Mechanism ◽  
Anaerobic Bacteria ◽  
Research Direction ◽  
Biohydrogen Production ◽  
Future Research ◽  
Hydrogen Energy ◽  
Industrialization Process ◽  
Catalytic Mechanisms

Hydrogenase plays an important role in the process of biohydrogen production. Hydrogenases have very unique active sites and are classified into three groups according to the metal composition of the active sites: the [Ni-Fe] hydrogenase, [Fe-Fe] hydrogenase, and [Fe-only] hydrogenase. In this paper, the crystal structures and active sites of three kinds of hydrogenases are examined and compared. These enzymes have an unusual structural feature in common. Their similar active site indicates that the catalytic mechanism of hydrogen activation is probably similar. The understanding of the catalytic mechanisms for the three kinds of hydrogenases may help achieve the industrialization process of hydrogen energy production. Moreover, the future research direction about the hydrogenases from auto-aggregative bacteria and the chemical mimic of hydrogenases structure is discussed.

scholarly journals Insights into the role of an Fe–N active site in the oxygen reduction reaction on carbon-supported supramolecular catalysts

RSC Advances ◽  
2020 ◽  
Vol 10 (15) ◽  
pp. 8709-8716
Author(s):  
Lin Gu ◽  
Yunyun Dong ◽  
Yan Zhang ◽  
Bo Wang ◽  
Qing Yuan ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Oxygen Reduction Reaction ◽  
Oxygen Reduction ◽  
Active Site ◽  
Active Sites ◽  
Reduction Reaction ◽  
Alkaline Media ◽  
Supramolecular Catalysts

The PPYTZ–Fe/C catalyst containing Fe–N active sites exhibited high ORR catalytic activity and stability in alkaline media with a four-electron pathway progress.

Direct templating assembly route for the preparation of highly-dispersed vanadia species encapsulated in mesoporous MCM-41 channel

RSC Advances ◽  
2015 ◽  
Vol 5 (88) ◽  
pp. 72099-72106 ◽  
Author(s):  
Fu Yang ◽  
Shuying Gao ◽  
Cuirong Xiong ◽  
Saifu Long ◽  
Xiaoming Li ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Active Sites ◽  
Highly Dispersed ◽  
Mcm 41

Understanding the nature of active sites, including the number and dispersion on the surface of a support, is essential to improve the catalytic activity.

scholarly journals A Kinetic Approach to Defining the Role of Chemically Modifiable Residues at the Active Sites of Enzymes

1975 ◽  
Vol 28 (4) ◽  
pp. 379
Author(s):  
Leonie K Ashman ◽  
D Bruce Keech
Keyword(s):  
Biological Activity ◽  
Catalytic Activity ◽  
Kinetic Analysis ◽  
Active Site ◽  
Initial Velocity ◽  
Active Sites ◽  
Kinetic Approach ◽  
Modified Enzyme ◽  
Enzyme Molecules

Initial velocity studies can be used to define the function of chemically modifiable residues in the active site of a multisubstrate enzyme. Since the method relies on measuring biological activity, it has the advantage that it can be used with small amounts of relatively impure enzyme, but requires that modified enzyme molecules have some residual catalytic activity. The kinetic analysis of the modified enzyme can be carried out in the presence of some unmodified enzyme molecules.

scholarly journals The inter-dimeric interface controls function and stability ofUreaplasma urealiticummethionine S-adenosyltransferase

2019 ◽  
Author(s):  
Daniel Kleiner ◽  
Fannia Shmulevich ◽  
Raz Zarivach ◽  
Anat Shahar ◽  
Michal Sharon ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Enzymatic Activity ◽  
Active Site ◽  
Active Sites ◽  
Structural Integrity ◽  
Functional Unit ◽  
Proteolytic Degradation ◽  
Interface Area ◽  
Dimeric Interface ◽  
Product Accumulation

SummaryMethionine S-adenosyltransferases (MATs) are predominantly homotetramers, comprised of dimers of dimers. The highly conserved dimeric interface harbors two active sites, making the dimer the obligatory functional unit. Yet, functionality of the recently evolved inter-dimeric interface remains unknown. Here, we show that the inter-dimeric interface ofU. urealiticumMAT has evolved to control the catalytic activity and structural integrity of the homotetramer in response to product accumulation. When all four active sites are occupied with the product, S-adenosylmethionine (SAM), binding of four additional SAM molecules to the inter-dimeric interface prompts a ∼45° shift in the dimer orientation and a concomitant ∼60% increase in the interface area. This rearrangement inhibits the enzymatic activity by locking the flexible active site loops in a closed state and renders the tetramer resistant to proteolytic degradation. Our findings suggest that the inter-dimeric interfaces of MATs are recruited by evolution to tune the molecular properties of the entire homotetramer.

scholarly journals Inactivation of horse liver mitochondrial aldehyde dehydrogenase by disulfiram. Evidence that disulfiram is not an active-site-directed reagent

1987 ◽  
Vol 242 (2) ◽  
pp. 499-503 ◽  
Author(s):  
C G Sanny ◽  
H Weiner
Keyword(s):  
Catalytic Activity ◽  
Aldehyde Dehydrogenase ◽  
Active Site ◽  
Active Sites ◽  
Specific Activity ◽  
Cysteine Residue ◽  
Complete Inactivation ◽  
Horse Liver ◽  
Inactivation Mechanism ◽  
Liver Aldehyde Dehydrogenase

The inhibition of mitochondrial (pI 5) horse liver aldehyde dehydrogenase by disulfiram (tetraethylthiuram disulphide) was investigated to determine if the drug was an active-site-directed inhibitor. Stoichiometry of inhibition was determined by using an analogue, [35S]tetramethylthiuram disulphide. A 50% loss of the dehydrogenase activity was observed when only one site per tetrameric enzyme was modified, and complete inactivation was not obtained even after seven sites per tetramer were modified. Modification of only two sites accounted for a loss of 75% of the initial catalytic activity. The number of functioning active sites per tetrameric enzyme, as determined by the magnitude of the pre-steady-state burst of NADH formation, did not decrease until approx. 75% of the catalytic activity was lost. These data indicate that disulfiram does not modify the essential nucleophilic amino acid at the active site of the enzyme. The data support an inactivation mechanism involving the formation of a mixed disulphide with a non-essential cysteine residue, resulting in a lowered specific activity of the enzyme.

scholarly journals Ammonia Decomposition Enhancement by Cs-Promoted Fe/Al2O3 Catalysts

2020 ◽  
Vol 150 (12) ◽  
pp. 3369-3376
Author(s):  
Luke A. Parker ◽  
James H. Carter ◽  
Nicholas F. Dummer ◽  
Nia Richards ◽  
David J. Morgan ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Induction Period ◽  
Active Site ◽  
Active Sites ◽  
Decomposition Reaction ◽  
Ammonia Decomposition ◽  
Site Analysis ◽  
Rate Determining Step ◽  
Equilibrium Conversion ◽  
On Line

Abstract A range of Cs-doped Fe/Al2O3 catalysts were prepared for the ammonia decomposition reaction. Through time on-line studies it was shown that at all loadings of Cs investigated the activity of the Fe/Al2O3 catalysts was enhanced, with the optimum Cs:Fe being ca. 1. Initially, the rate of NH3 decomposition was low, typically < 10% equilibrium conversion (99.7%@500°C) recorded after 1 h. All catalysts exhibited an induction period (typically ca. 10 h) with the conversion reaching a high of 67% equilibrium conversion for Cs:Fe = 0.5 and 1. The highest rate of decomposition observed was attributed to the balance between increasing the concentration of Cs without blocking the active site. Analysis of H2-TPR and XPS measurements indicated that Cs acts as an electronic promoter. Previously, Cs has been shown to act as a promoter for Ru, where Cs alters the electron density of the active site, thereby facilitating the recombination of N2 which is considered the rate determining step. In addition, XRD and N2 adsorption measurements suggest that with higher Cs loadings deactivation of the catalytic activity is due to a layer of CsOH that forms on the surface and blocks active sites. Graphic Abstract

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