Iron carboxylate groups

When PMMA was adsorbed onto an iron substrate, four components were not sufficient to explain the C(ls) spectrum (see Fig. 21b) and a fifth component had to be added at 288.1 eV as shown in Fig. 21c. This component was attributed to carboxyl groups, indicating that the ester groups were partially hydrolyzed. Similarly, Leadley and Watts found that there were five components in the C(ls) spectrum of PMMA spin-coated onto aluminum, copper, and nickel substrates 124]. 

The presence of sulphonic and carboxylic groups enables the iron ions to be in the vicinity of the cellulose backbone chain. In this case, the radicals formed can easily attack the cellulose chain leading to the formation of a cellulose macroradical. Grafting of methyl methacrylate on tertiary aminized cotton using the bi-sulphite-hydrogen peroxide redox system was also investigated [58]. 

Maleic and fumaric acids are cis- and irons- Maleic acid gives up its first proton more readily isomers having two carboxyl groups, than does fumaric acid. However, the opposite... 

A catalytic mechanism, which is supported by deuterium-labeling experiments in the corresponding Ru-catalyzed procedure [146], is shown in Scheme 47. Accordingly, the reactive Fe-hydride species is formed in situ by the reaction of the iron precatalyst with hydrosilane. Hydrosilylation of the carboxyl group affords the 0-silyl-A,0-acetal a, which is converted into the iminium intermediate b. Reduction of b by a second Fe-hydride species finally generates the corresponding amine and disiloxane. 

Fig. 1. The schematic structure of basic iron carboxylates. R is an alkyl or aryl group. (Reproduced from Ref. 5b. Copyright 1987 American Chemical Society.)...

Early attempts to purify the enzyme brought the quick realization that aconitase is easily inactivated (6,7). In the early 1950 s Dickman and Qoutier (8,9) found that inactivated aconitase could be reactivated by incubation with iron and a reduc-tant. From kinetic analyses of the iron and reductant effects on enzyme activity, Morrison argued that both formed Michaelis-Menten complexes wiA the enzyme (10). This refuted the earlier idea that the sole role of the reductant was to maintain iron in a reduced state (9). Of several metal cations tried, only ferrous ion was found to be capable of this reactivation process (8,11). Because of the absolute requirement for iron in activation, the known chelation properties of citrate, and Ogston s 3-point attachment proposal, Speyer and Dickman proposed that the active site iron provides three coordination sites for substrate binding - one for hydroxyl and two for carboxyl groups (12). 

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