Detoxification center

Most intoxicated individuals do not need hospitalization, display none of the previous medical problems, and experience minimal withdrawal symptoms. Observing and treating them in the emergency room or a nonmedical detoxification center (i.e., social intoxication) for 6 to 12 hours may be all that is required. 

We also demonstrated in this study that FAEE synthase activity could be induced nearly twofold in the WBC fraction of humans ingesting 2 oz of scotch whiskey for 6 d (Gorski. 1996). This supports the conclusion that FAEE synthase is regulated to some extent by the presence of ethanol. Ihe enzyme activity returned to baseline levels despite ingestion of 2 oz of scotch whiskey for an additional 3 d. In this report, it was also shown that alcoholic individuals have approximately half the WBC FAEE synthase activity detected in normal controls. The lower enzyme activity observed in the WBCs of alcoholics in a detoxification center may be the result of years of ethanol abuse, or it may be that alcoholics congenitally have low levels of FAEE synthase. If the latter is true, this finding may explain, in part, the genetic predisposition of many alcoholic individuals to ethanol abuse. 

The mechanism resembles that proposed for a phosphotriesterase (Fig. 12-24). The triesterase catalyzes detoxification of organophosphorus toxins such as parathion (Box 12-E) and seems to have evolved rapidly from a homologous protein of unknown function.721 The phosphotriesterase contains two Zn2+ ions in a dimetal center. An unusual structural feature is a carbamate group, formed from Lys 169 and C02, which provides a bridging ligand for the metal pair.721-725 A carbamylated lysine also functions in ribulose bisphos-phate carboxylase (Fig. 13-11). 

In various species of bacteria several different types of non-assimilatory nitrite reductases are found. Escherichia coli has a cytoplasmic NAD(P)H-dependent enzyme whose role seems to be detoxification of nitrite. This type of enzyme, coded for by the nirB gene, also contains siroheme as the redox active catalytic center (Cole, 1988). Additionally in E. coli, and expressed under different conditions to the cytoplasmic enzyme, is a periplasmic nitrite reductase that catalyses formation of ammonia from nitrite (Cole, 1988). This enzyme has five c-type (Figure 1) hemes per polypeptide chain one of these hemes, the catalytic site, has the unique CXXCK sequence as its attachment site (Einsle et al., 1999). Electrons reach this type of nitrite reductase, which is fairly widely distributed amongst the microbial world, from the cytoplasmic membrane electron transfer chain. The exact electron donor partner from such chains for this type of nitrite reductase is unknown (Berks et al., 1995). 

Superoxide Reductase (see Iron Proteins with Mononuclear Active Sites). Detoxification of reactive oxygen species in anaerobic microorganisms has recently been shown to center around SOR, a novel mononuclear iron enzyme that reduces superoxide to hydrogen peroxide (see equation 4), rather than dismuting superoxide to oxygen and hydrogen peroxide as is the case for the superoxide dismutases found in aerobic organisms. 

The first large scale applications of solar waste water detoxification are being tested in the US and in Spain. Researchers of the Sandia National Laboratory are testing Ti02-suspensions in a plant in New Mexico, and various European groups are using the test center in Almeria in Spain. 

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