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Substrate appearance

In the hydrolysis of acridine antimalarials, the role of the protonated species of the substrate appeared to be important even in aqueous solution buffered at pH 7.3, i.e., under conditions of physiological interest.Moreover, out of the three possible modes of reaction mathematically possible (H3O+-HB, HgO-f BH+, and OH -f BH2+, where B is the basic substrate) the one not involving the protonated substrate can be ruled out on structural grounds. [Pg.297]

Chiral and achiral Jacobsen s catalysts exhibit similar diatereomeric excesses during the diastereoselective epoxidation of R-(+)-limonene using in situ prepared oxidizing agents. Therefore, the chiral center of the substrate appears to govern the chiral induction. In contrast, the chirality of the Jacobsen s catalyst appears to be responsible for the chiral induction when commercially available oxidants were used. [Pg.483]

Further work supported these observations but seemed to draw a clear distinction between metals such as Au, Pt and Ag other cathodes in that the predominant products at the former substrates appeared to be only those observed by Haynes and Sawyer (1967). In contrast, oxalate formation was favoured by most other metals. [Pg.296]

Brain ChAT has a KD for choline of approximately 1 mmol/1 and for acetyl coenzyme A (CoA) of approximately 10pmol/l. The activity of the isolated enzyme, assayed in the presence of optimal concentrations of cofactors and substrates, appears far greater than the rate at which choline is converted to ACh in vivo. This suggests that the activity of ChAT is repressed in vivo. Surprisingly, inhibitors of ChAT do not decrease ACh synthesis when used in vivo this may reflect a failure to achieve a sufficient local concentration of inhibitor, but also suggests that this step is not rate-limiting in the synthesis of ACh [18-20]. [Pg.192]

It has also been shown that the CYP4 family contains a number of natural substrates appear to be arachidonic acid, the prostaglandins, and/or the leukotrienes. For example, CYP4F2 and CYP4F3, isolated from human liver and human leukocytes, respectively, are leukotriene B4 -hydroxylation of arachidonic acid to form 20-hydroxy-5, 8, 11, 14-eicosatetraenoic... [Pg.68]

As previously mentioned, the first atomic layer, in contact with the substrate, appears to be the most critical. Electrochemically there are three different ways to form the first atomic layer of Se, and graphs depicting each are displayed in Fig. 56. The first method is straightforward—the direct reductive deposition of Se atomic layers from a HSeOs" solution. The voltammetry for Se deposition is shown in Fig. 57 and displays two feature, Ci and Cj. Ci could be thought of as a UPD feature because it... [Pg.167]

The pattern of microbial hydroxylation of aromatic substrates appears to occur generally according to the usual rules of electrophilic aromatic substitution as shown by the hydroxylation positions of acronycine (1) at C-9 and C-11 (para- and ortho-positions to the amino group and mefa-position to the car-... [Pg.194]

However, various assays utilizing nonstandardized sources of HDAC protein preparations and substrates appear to generate large variations in the resulting data. As an example. Table 6.1 summarizes the observed variations in the recently reported in vitro data for the effects of SAHA on individual H DAC isoforms [14,19-23]. HDAC isoforms used for in vitro screening assays have been expressed in Escherichia coli (HDACl, 3), Picchia, SF9 insect cells (HDACl-11) or mammalian cells (recombinant HDACl, 3) these sources may lead to differential enzyme activities. [Pg.121]

The investigation of the exact ECS of small particles adsorbed on a flat (monociystalhne) substrate appears to be an excellent way to determine the relative orientation dependence of y(0) and from there the relative step and step interaction energies, provided the ECS exhibits all orientations, such that the conversion to y(0) is unique [1-4]. In that sense ECS studies are an important supplement to studies of transient morphological shapes which normally yield the product of mobility x energy. [Pg.48]

For dinuclear Cu complexes, several pathways are possible as summarized in Scheme 15 [182]. In addition, plausible alternatives involve mixed-valent Cu Cu species where only one of the Cu ions is directly involved in the electron transfer. The latter seems most hkely in cases where the substrate binds to only one of the two copper ions, and H2O2 may then form upon oxidation of the Cu Cu -semiquinone intermediate [195]. Different coordination modes of the DTBC substrate appear to be indeed possible, depending on the particular dicopper scaffold [133,196,197]. Unfortunately, detailed mechanistic studies are still quite scarce [198-203] and most proposed catalytic pathways are rather speculative. [Pg.55]

Processes for two-electron reductions, two sequential one-electron reductions with a radical anion intermediate, and reactions of dianions with unreduced parents to give radical anions were observed. Structural reorganization is occasionally observed, particularly in the case of Fe(CO)2 and Fe(CO)3 complexes (26). There appears to be little correlation between structure and electrochemical behavior. In general, the presence of metal-metal bonds in the substrate appears to correlate well with the ability to yield a stable radical anion on reduction. The lack of a metal-metal bond correlates, although poorly, with the ability to form radical cations (25). At present, the predictability of results from reduction in metal-carbonyl complexes is very low. The area remains one in which a great deal more work is needed. [Pg.311]

In listing the ways in which metal ions may promote organic reactions, the requirement that the metal ion be suitably positioned within the substrate molecule was emphasized. Specific complexation or chelation of the metal ion with the substrate appears to be an absolute requirement of metal ion catalysis. In many cases chelation appears to be the rule, which usually means that the substrate must contain a donor atom in addition to the reactive center of the molecule with which the metal ion also complexes, or must contain two donor atoms in addition to the reactive center. Many attempts have been made to correlate the effectiveness of catalysis by a series of metal ions with the relative formation constants of the complexes. Such correlations have been successful in a number of reactions, but unsuccessful in others. In the successful correlations the complex chosen for the correlation closely approximates the transition state of the reaction. This indicates that the metal ion complex must stabilize the transition state of the reaction in order to assist the reaction effectively, and that metal ion complex formation in the ground state can have an effect exactly opposite to that of catalysis, since in such a case the ground state becomes stabilized. [Pg.39]

Chemical Inhibition. A large variety of chemical compounds have been added to milk or purified lipase. The conditions under which the inhibitor is studied are very important. Factors such as pH, temperature, time of addition of the chemical, sequence of addition of reactants, and the presence or absence of substrate are undoubtedly involved. The presence of substrate appears to offer some degree of protection to the enzymes. Consequently, in lipase studies, the surface area of the emulsified substrate is probably also important. [Pg.229]

Steric bulk of the substrates appears to play a role in determining which product is formed, but the key factor that favors formation of the cyclic product is the presence of a base cocatalyst, such as Et3N or DBU. Although silylformylation can occur for certain substrates when a base is part of the reaction mixture, in the absence of a base only silylformylated products are obtained. The silyl group always adds to the terminal carbon of the acetylene in the formation of either product. [Pg.238]

The technique of producing ordered layers of amphiphilic materials by evaporation in vacuo on to a suitable substrate appears to originate in the work of Agarwal [18] but has only very recently been developed. [Pg.4]

A thin film of SA APS on a zinc substrate appears to be highly oriented with the vinylbenzyl groups away from the surface. The orientation is much less pronounced in a thick film. [Pg.342]

Since Si02 substrates appear frequently during IC fabrication, the adhesion test results for this substrate are important. Four types of oxides have been extensively tested. They are (1) thermal oxide grown at 7>1000°C, (2) softer oxide processed by conventional spin-on-glass technology, (3) phosphorus-doped LPCVD oxide, and (4) low-temperature (200°C) plasma deposited oxide. [Pg.453]

Peptide substrates have been shown to bind to the apoenzyme and protect it from reactivation with metal ions (98, 99). The apoenzyme-substrate complexes were estimated to have about the same stabilities as the corresponding complexes with the native enzyme. On the other hand, ester substrates appear to require the presence of the metal ion for binding. Metallocarboxypeptidases, including the inactive Cu(II) enzyme, form complexes with both kinds of substrates hindering the dissociation of the metal ion. [Pg.181]

The immediate changes in UV spectra57 exhibited by the substrates on addition of mineral acids are consistent with a rapid protonation equilibrium, S+H+ < SH+, to form the conjugated acid. In order to interpret the rate data, one must first correct the observed values of k,j, for the amount of protonated substrate. Spectrophotometric methods are widely applicable for determination of the ionization ratio, I = CSH+ /Cs, of moderately basic substrates74. For A-f-butylbenzaldoxime and 2-/-butyl-3-phenyloxaziridinc, however, the rate of the hydrolysis reaction (t /2 = 1 min) at the maximum in the profile at 24.2 °C made it impossible to measure the zero-time absorption of the substrates. However, allowing for medium effects in the absorption spectra, the substrates appeared to be essentially fully protonated in solutions of CH+ > 2 M in all three acids. [Pg.322]


See other pages where Substrate appearance is mentioned: [Pg.311]    [Pg.1339]    [Pg.354]    [Pg.426]    [Pg.491]    [Pg.77]    [Pg.161]    [Pg.615]    [Pg.143]    [Pg.356]    [Pg.170]    [Pg.213]    [Pg.61]    [Pg.96]    [Pg.323]    [Pg.176]    [Pg.1026]    [Pg.964]    [Pg.223]    [Pg.575]    [Pg.240]    [Pg.248]    [Pg.203]    [Pg.1163]    [Pg.77]    [Pg.183]    [Pg.33]    [Pg.65]    [Pg.97]    [Pg.162]   
See also in sourсe #XX -- [ Pg.182 ]




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