Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Substrates activation

A fundamental issue in selective oxidation is the activation of C—H bonds that is always required for ODH (oxidative dehydrogenation) and oxo-functionalization and is detrimental for epoxidation. A particular case is silver [70] as catalyst, which can achieve highly selective epoxidation of ethene as well as highly selective dehydrogenation of methanol to formaldehyde although it is notably in both cases only the same metallic catalyst. We will return to this case in the next section, which deals with the multiplicity of active oxygen species. [Pg.7]

The issue of C—H activation has been addressed many times in the literature. It is common ground to state that the initial C—H activation should be the ratedetermining step in the overall process of selective oxidation. This statement can be verified under conditions of proper kinetic studies when limited conversions and small concentrations of reducing products leave the catalyst in its original and active state and when no substantial re-adsorption or site-blocking of products occur. [Pg.7]

A prototype study for this issue was performed for the conversion of ethane to acetic acid [71] and the same group highlighted in an earlier comparative study of C3 oxidation [54] that, although initial propane activation is a difficult step, subsequent reactions associated with either excessive residence times of intermediates or with branching of reaction sequences into total oxidation may interfere with the overall selectivity to partial oxidation products. [Pg.8]

The fact that the active site is already partly reduced will diminish its ability (nucleophilicity) to activate all C—H bonds. In this way the oxygen activation on a site that is partly reduced will create a situation in which oxygen transfer can occur selectively without simultaneous activation of many reactive sites at the alkoxide. Obviously, for such a fortunate situation no external regeneration of the active site by lattice oxygen or by withdrawal of electrons to distant electron sinks (phase cooperation) must occur. The concept of site isolation finds in such an interpretation a natural cause a catalytic site must be constructed in such a way that its electronic structure is allowed to fluctuate between a highly active initial state and moderate consecutive states as the conversion of the substrate molecule proceeds. The site is [Pg.11]

In the literature [109] on homogeneous C—H bond activation substantial evidence exists for selective radical activation using nitrogen-containing non-metallic [Pg.13]


Enzymatic reactions frequently undergo a phenomenon referred to as substrate inhibition. Here, the reaction rate reaches a maximum and subsequently falls as shown in Eigure 11-lb. Enzymatic reactions can also exhibit substrate activation as depicted by the sigmoidal type rate dependence in Eigure 11-lc. Biochemical reactions are limited by mass transfer where a substrate has to cross cell walls. Enzymatic reactions that depend on temperature are modeled with the Arrhenius equation. Most enzymes deactivate rapidly at temperatures of 50°C-100°C, and deactivation is an irreversible process. [Pg.838]

The reaction of 1,2,4-triazine 4-oxides 55 with CH-active 1,3-diketones (dime-done, indanedione, iV.iV -dimethylbarbituric acid) in the presence of trifluoroacetic acid (substrate activation by protonation) or KOH (activation of the nucleophile) leads to stable cr -adducts 63, whose oxidative aromatization by the action of KMn04 results in 5-substituted 1,2,4-triazine 4-oxides 64 (98MI). [Pg.277]

Figure 9-3. Conventional multilayer light emission device (LED) indium tin oxide (ITO) electrode on a substrate, active layers A (hole transport), B (emitter), C (electron transport), and a niclat electrode. A possible encapsulation layer has been omitted, which would prevent the conjugated molecules from photo-oxidation. Figure 9-3. Conventional multilayer light emission device (LED) indium tin oxide (ITO) electrode on a substrate, active layers A (hole transport), B (emitter), C (electron transport), and a niclat electrode. A possible encapsulation layer has been omitted, which would prevent the conjugated molecules from photo-oxidation.
Dual activation of nucleophile and epoxide has emerged as an important mechanistic principle in asymmetric catalysis [110], and it appears to be particularly important in epoxide ARO reactions. Future work in this area is likely to build on the concept of dual substrate activation in interesting and exciting new ways. [Pg.266]

Toxin Protein substrate Activity Functional consequences... [Pg.246]

FIGURE 12.1 Effects of substrate (reactant) concentration on the rate of enzymatic reactions (a) simple Michaelis-Menten kinetics (b) substrate inhibition (c) substrate activation. [Pg.437]

As written, this rate equation exhibits neither inhibition nor activation. However, the substrate inhibition of Example 12.1 occurs if 2 = 0, and substrate activation occurs if k = 0. [Pg.439]

In this section we deal with reactions in which in one step, formally an O-H bond activation, is involved. Although the precise reaction mechanisms have not been elucidated, some of these reactions are considered to proceed by nucleophilic attack of water, an alcohol, etc. to a substrate activated by a transition metal. We choose to emphasize examples coming from our own research activities in this field. [Pg.193]

Woolridge, E. M. Rokita, S. E. 6-(Difluoromethyl)tryptophan as a probe for substrate activation during the catalysis of tryptophanase. Biochemistry 1991, 30, 1852-1857. [Pg.325]

This study supports rate-determining H-OH bond breaking, which constrasts with previous reports that identified vinylidene isomerization as the key step in catalytic alkyne activation. The results indicate an enzyme-like mechanism is operative involving cooperative substrate activation by a metal center and proximal hydrogen bond donor/acceptors. In the future we will apply these principles to the activation of additional species. [Pg.240]

The four oxygen donor atoms preorganized in a quasiplanar geometry have a major effect in determining the set and relative energy of the frontier orbitals available at the metal for the substrate activation (see Chart 2). [Pg.169]

Friedrichsen, G. M., etal. Synthesis of analogs of L-valacyclovir and determination of their substrate activity for the oligopeptide transporter in Caco-2 cells. Pur. J. Pharm. Sci. 2002, 26, 1-13. [Pg.273]

Substrate Activity [pmol min 1 mg-1 protein] Intestine Liver Reference... [Pg.317]

Haem, Fe Chlorophyll, Mg Coenzyme B12, Co Factor F-430, Ni Electron transfer in membranes and elsewhere Light capture and transduction in membranes Transfer of methyl, rearrangements of substrates Activation of carbon monoxide... [Pg.216]

Substrates may affect enzyme kinetics either by activation or by inhibition. Substrate activation may be observed if the enzyme has two (or more) binding sites, and substrate binding at one site enhances the alfinity of the substrate for the other site(s). The result is a highly active ternary complex, consisting of the enzyme and two substrate molecules, which subsequently dissociates to generate the product. Substrate inhibition may occur in a similar way, except that the ternary complex is nonreactive. We consider first, by means of an example, inhibition by a single substrate, and second, inhibition by multiple substrates. [Pg.270]

The cleavage of catechols with the incorporation of oxygen is clearly favored in the presence of some of the iron(III) complexes as catalysts. Que and co-workers proposed a substrate activation mechanism for these reactions, wherein the delocalization of the unpaired spin density... [Pg.422]

A recent report on a NR2B selective NMDA receptor antagonist (9) supports the findings of Kalvass and Maurer [56], Rapid equilibration between plasma and CNS coupled with the lack of Pgp substrate activity led the authors to assume that plasma-free and brain-free drug concentrations were equivalent. An ex vivo receptor binding assay showed 50% occupancy at a total plasma concentration of 230 nM. Given a rat-free fraction of 15.3%, the authors concluded that 50% brain occupancy occurred at 35 nM unbound brain concentration, which was in reasonable agreement with the measured Ki of 3.4 nM versus the human receptor. [Pg.497]

Silverman has pointed out that several criteria must be met to demonstrate that a compound is a true suicide substrate 1101 (1) Loss of enzyme activity must be time-dependent, and it must be first-order in [inactivator] at low concentrations and zero-order at higher concentrations (saturation kinetics), (2) substrate must protect the enzyme from inactivation (by blocking the active site), (3) the enzyme must be irreversibly inactivated and be shown to have a 11 stoichiometry of suicide substrate active site (dialysis of enzyme previously treated with radiolabeled suicide substrate must not release radiolabel into the buffer), (4) the enzyme must unmask the suicide substrate s potent electrophile via a catalytic step,1121 and (5) the enzyme must not be covalently labeled with the activated form of the suicide substrate following its escape from the active site (the presence of bulky scavenging thiol nucleophiles in the buffer must not decrease the observed rate of inactivation). [Pg.360]

Chetty SC, Aldous CN, Rashatwar SS, et al. 1983b. Effect of chlordecone on pH- and temperature-dependent substrate activation kinetics of rat brain synaptosomal ATPases. Biochem Pharmacol 32(21 ) 3205-3211. [Pg.244]

In the literature, there are numerous reports regarding the interactions between amines and both electron and proton acceptors132, but less attention has been devoted to interactions between amines and aromatic electron acceptors, in particular when the substrate/amine system is a reacting system, as in the case of nucleophilic aromatic substitution (SjvAr) reactions between amines and substrates activated by nitro or by other electron-withdrawing groups. [Pg.460]

PFK-1 is a classic example of a tetrameric allosteric enzyme. Each of the four subunits has two ATP binding sites one is the active site where ATP is co-substrate and the other is an inhibitory allosteric site. ATP may bind to the substrate (active) site when the enzyme is in either the R (active) or T (inhibited) form. The other co-substrate, F-6-P binds only to the enzyme in the R state. AMP may also bind to the R form and in so doing stabilises the protein in that active conformation permitting ATP and F-6-P to bind. [Pg.73]

Song, E.S., Juliano, M.A., Juliano, L., and Hersh, L.B., Substrate activation of insulin-degrading enzyme (insulysin). A potential target for drug development, /. Biol. Chem., 278, 49789, 2003. [Pg.239]

Evans, J.P., Ahn, K. and Klinman, J.P. (2003). Evidence that dioxygen and substrate activation are tightly coupled in dopamine (3-monoxygenase. J. Biol. Chem. 278, 49691-49698... [Pg.78]


See other pages where Substrates activation is mentioned: [Pg.319]    [Pg.328]    [Pg.226]    [Pg.438]    [Pg.48]    [Pg.48]    [Pg.49]    [Pg.67]    [Pg.900]    [Pg.476]    [Pg.448]    [Pg.99]    [Pg.310]    [Pg.207]    [Pg.315]    [Pg.535]    [Pg.168]    [Pg.161]    [Pg.355]    [Pg.442]    [Pg.448]    [Pg.64]    [Pg.70]    [Pg.341]    [Pg.200]    [Pg.619]    [Pg.66]   
See also in sourсe #XX -- [ Pg.437 ]

See also in sourсe #XX -- [ Pg.81 ]

See also in sourсe #XX -- [ Pg.437 , Pg.438 , Pg.439 ]

See also in sourсe #XX -- [ Pg.838 ]

See also in sourсe #XX -- [ Pg.13 ]

See also in sourсe #XX -- [ Pg.1395 ]

See also in sourсe #XX -- [ Pg.282 ]

See also in sourсe #XX -- [ Pg.114 ]




SEARCH



1,4-addition active substrate control

Activated aromatic substrates

Activated substrates

Activated sugar-nucleotide substrate

Activation energies substrates

Activation of Substrates with Non-Polar Single Bonds

Activation of Substrates with Polar Single Bonds

Activation of a Substrate toward Nucleophilic Attack

Activation of substrate

Activation of the carbonyl substrate

Activation unsaturated substrates

Activator-substrate-depletion system

Active Sites and Substrate Binding Models

Active methylene substrates

Active site mapping with substrate analogs

Active site-substrate complexes

Active site-substrate complexes computer-generated

Active transport of substrate

Active-site substrate

Active-site-directed Irreversible Inhibitors and Substrates

Activity Measurements of Proteinases Using Synthetic Substrates

Activity with Branched Substrates

Anionic substrate activation

Carbonic anhydrase substrate activation

Catalytic activity catalyst substrate

Catalytic properties substrate active states

Catechol dioxygenases substrate activation

Cholinesterases substrate activation

Chymotrypsin active center amino substrate specificity

Cofactor-Independent with Activated Substrates

Computer generated active site-substrate

Control mechanisms precursor substrate activation

Direct Functionalization via C-H Activation of Heterocyclic Substrates

Dual activation, substrate

Enzyme activation single-substrate reaction

Enzyme activation substrate complex

Enzyme activity substrate concentration affecting

Factor active site substrate sequences

Heterolytic Activation of Substrate

High activity substrates

High-Throughput Screening for Carboligation Activity with the Substrates Benzaldehyde and Dimethoxyacetaldehyde

Intramolecular C-H Activation of Heterocyclic Substrates

Mitogen-activated protein kinase substrate specificity

Optically active substrates

Oxidative activation 3 substrates

Peaches substrate activity

Peptidase Activity Assays Using Protein Substrates

Phenolic antioxidant activity substrates used

Precedents for Metal Activation of Organic Substrates

Protein Engineering to Improve Enzymatic Activity and Alter Substrate Specificity

Raman scattering active substrate

Reactions of Redox-Activated Complexes with Gaseous Substrates

Releasing the Spring Cofactor- and Substrate-assisted Activation of Factor IXa

SERS-Active Substrates

Specific Amino Acids at the Active-Site Involved in Catalysis and Substrate Binding

Substrate Conformational Transition and the Role of Active Site Residues

Substrate Scope, Activity, and Enantioselectivity

Substrate activation catalysis

Substrate activation transition metal complexes

Substrate activity screening

Substrate binding active ternary complex

Substrate binding at an active site

Substrate dependence, enzyme activity

Substrate preparation activation

Substrate transport observed activation energies

Substrate-activator complex

Substrates activity

Substrates phosphatase activity measurement

Substrates/products inhibition/activation

Surface Activity of Polyethers on Copper and Tin Substrates

The Selective Activation of Alternative Reaction Sites in Substrates

Virus Sialidase Substrate Binding and Active Site

Xanthine oxidase substrate activity

© 2024 chempedia.info