Imidazole modification with

With sUght modifications of these conditions it is possible to prepare mono N-substituted imidazoles (Scheme 5), the reaction working well with aliphatic amines but not with many aromatic amines. The imsymmetrical... 

A traditional system for the preparation of table olives, involves a treatment of the fresh fruit with a solution of NaOH to hydrolised the bitter glycoside oleuropein, followed by a lactic fermentation in brine. The modifications that take place on pectic polysaccharides of olives (Manzanilla variety) during this process was smdied. Processing induced a net loss of polysaccharides soluble in sodium carbonate and a paralel accumulation of water and Imidazole/HCl soluble polysaccharides. A general decrease of the apparent molecular weight of water and carbonate soluble polysaccharides was also detected. 

Several modifications of procedures based on halophosphonium ion have been developed. Triphenylphosphine and imidazole in combination with iodine or bromine gives good conversion of alcohols to iodides or bromides.22 An even more reactive system consists of chlorodiphenylphosphine, imidazole, and the halogen,23 and has the further advantage that the resulting phosphorus by-product diphenylphosphinic acid, can be extracted with base during product workup. 

A modification of this method, related to the Beckmann rearrangement, entails treatment of a ketoxime with one equivalent of CDI, then four to five equivalents of a reactive halide such as allyl bromide or methyl iodide (R3X) under reflux in acetonitrile for 0.5-1.5 h. Quatemization of the imidazole ring effectively promotes the reaction by increasing the electron-withdrawing effect. The target amides then are obtained by hydrolysis. High yields, neutral conditions, and a very simple procedure make this modification of the synthesis of amides by azolides a very useful alternative. 1243... 

The process of modification is shown in Fig. 13. Lys-52 is first derivatized with 4-thiobutanal and then a catalytic imidazole is bonded through a disulfide bridge into the active site. This can now act as a general base/nucleophile in the hydrolysis of [42], as was verified first by the pH-rate profile and then by complete deactivation of the antibody by diethyl pyrocarbonate (an imidazole-specific inactivating reagent). 

The standard ruthenium modification procedure involves the reaction of aquopentaammineruthenium(II) (ajRu " ) with the imidazole of a surface histidine of a protein [5, 13, 14]. The a5Ru(histidine)-modified proteins are stable in both the Ru(II) and the Ru(III) oxidation states and, although ajRu slowly dissociates from surface histidines [15], the ajRu complex stays attached for at least two months under appropriate conditions [16]. 

This general approach has, however, serious limitations. The position of the site for attack (and therefore the electron transfer distance involved) is very conjectural. In addition, the vexing possibility, which we have encountered several times, of a dead-end mechanism (Sec. 1.6.4) is always present. One way to circumvent this difficulty, is to bind a metal complex to the protein at a specific site, with a known (usually crystallographic) relationship to the metal site. The strategy then is to create a metastable state, which can only be alleviated by a discernable electron transfer between the labelled and natural site. It is important to establish that the modification does not radically alter the structure of the protein. A favorite technique is to attach (NH3)5Ru to a histidine imidazole near the surface of a protein. Exposure of this modified protein to a deficiency of a powerful reducing agent, will give a eon-current (partial) reduction of the ruthenium(III) and the site metal ion e.g. iron(III) heme in cytochrome c... 

The mechanism in Fig. 14 applies equally well to both PVC and HPll. However, an unusual bond between the imidazole ring of His392 and the p-carbon of Tyr415 on the proximal side of the HPll heme has been identified (Fig. 13) (93), and subsequently its presence was correlated with heme oxidation. The apparent correlation between heme oxidation and His-Tyr bond formation suggested a mechanistic linkage between the two modifications and an alternate mechanism imique to HPll was proposed (Fig. 15). As with the first mechanism, the reaction assumes the formation of compound I that is available for reduction. Formation of the His-Tyr bond, involving a base catalyzed proton extraction from the... 

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