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Iron derivatives, inactive

It was anticipated that a C4 -trialkyIstannyl group would intercept the C4 radical and result in loss of antimalarial activity. Indeed, 31 and 32 were inactive and iron(II) degradation afforded two major products in which the stannyl group had been eliminated (Scheme 6). They proposed that the deoxo derivative 33 was produced by elimination of a... [Pg.1290]

Titanium(IV)-porphyrin [TiO(TPP)] as well as molybdenum(V)-porphyrin [MoO(OMe)(TPP)] complexes were found to be active for the catalytic epoxidation of alkenes by alkyl hydroperoxides, whereas their peroxo derivatives are inactive.632 Iron(III)-porphyrin-peroxo complexes such as Fe(TPP)02NMe4 did not react with hydrocarbons, but form sulfato complexes upon reaction with S02.632 Manganese(III)-porphyrin-peroxo complexes Mn(02)(TPP) K+ were recently characterized by X-ray crystallography.634... [Pg.397]

A cofactor can be extracted from the iron-molybdenum protein, using Af-methylformamide. This cofactor (called FeMoCo) has many spectroscopic properties in common with the native protein, especially the EXAFS spectrum, and activates the inactive large protein derived from Azobacter vinelandii UW45 mutant which cannot incorporate molybdenum. The cofactor contains no protein or peptide, but does contain molybdenum, iron, and sulfur in atomic ratios of 1 6-8 4-9. It is believed to contain the dinitrogen-binding site (presumably molybdenum) but there is no definitive proof of this. [Pg.273]

Tannic acid has been reported to inhibit the formation of hydroxyl radical by chelation of Fe2+ [16], Because tannic acid is a plant-derived material, it and other natural polyphenols may be important for subsurface applications of Fenton chemistry. A study of 50 different iron chelators assessed the affect of each chelator on the Fenton process initiated with Fe3+ and hydrogen peroxide [17]. Among the nine classes of chelators tested, results indicated that the chelators ranged from inactive to highly active in terms of hydroxyl radical formation. [Pg.178]

Carbon forms play important roles as intermediates, catalyst additives and deactivating species in Fischer-Tropsch synthesis on iron catalysts. Deactivation may be due to poisoning or fouling of the surface by atomic carbidic carbon, graphitic carbon, inactive carbides or vermicular forms of carbon, all of which derive from carbidic carbon atoms formed during CO dissociation (ref. 5). While this part of the study did not focus on the carbon species responsible for deactivation, some important observations can be made to this end. [Pg.219]

R—N(CH3)2. This amine is demethylated and oxidized by cytochrome P-450 into a metabolite, probably the nitroso derivative (R—N=0), which forms a stable, inactive complex with the iron (Fe ) of cytochrome P-450 [115]. This complex prevents the enzyme from metabolizing other drugs any further [116]. These inactive complexes have been found in patients taking erythromycin. However, not all macrolides have been associated with the formation of these complexes [117]. The enzyme CYP3A4 appears to be most susceptible to inhibition by the macrolide antibiotics. This binding to and reduction in CYP3A4 activity is the... [Pg.351]

The purple acid phosphatases can occur in two diferric forms—one as the tightly bound phosphate complex (characterized for the bovine and porcine enzymes) (45, 171, 203) and the other derived from peroxide or ferricyanide oxidation of the reduced enzyme (thus far accessible for only the porcine enzyme) (206). These oxidized forms are catalytically inactive. They are EPR silent because of antiferromagnetic coupling of the two Fe(IIl) ions and exhibit visible absorption maxima near 550-570 nm associated with the tyrosinate-to-Fe(III) charge-transfer transition. The unchanging value of the molar extinction coefficient between the oxidized and reduced enzymes indicates that the redox-active iron does not contribute to the visible chromophore and that tyrosine is coordinated only to the iron that remains ferric in agreement with the NMR spectrum of Uf, (45). [Pg.161]


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Inactive

Iron derivatives

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