Biodegradation of monoaromatic hydrocarbons in aquifer columns amended with hydrogen peroxide and nitrate

The ability of indigenous microorganisms to degrade benzene, toluene, ethylbenzene and xylenes (BTEX) in laboratory scale flow-through aquifer columns was tested separately with hydrogen peroxide (110 mg/l) and nitrate (330 mg/l as NO₃⁻) amendments to air-saturated influent nutrient solution. The continuous removal of individual components from all columns relative to the sterile controls provided evidence for biodegradation. In the presence of hydrogen peroxide, the indigeneous microorganisms degraded benzene and toluene (> 95%), meta- plus para-xylene (80%) and ortho-xylene (70%). Nitrate addition resulted in 90% removal of toluene and 25% removal of ortho-xylene. However, benzene, ethylbenzene, meta- and para-xylene concentrations were not significantly reduced after 42 days of operation. Following this experiment, low dissolved oxygen (< 1 mg/l) conditions were initiated with the nitrate-amended column influent in order to mimic contaminated groundwater conditions distal from a nutrient injection well. Toluene continued to be effectively degraded (> 90%), and more than 25% of the benzene, 40% of the ethylbenzene, 50% of the meta- plus para-xylenes and 60% of the ortho-xylene were removed after several months of operation.     

Reverse short channel effects in high-k gated nMOSFETs

Anomalous threshold voltage roll-up behavior, commonly referred as reverse short channel effect (RSCE), has been observed in high-k (HfO₂ on SiON buffer, Al₂O₃ on SiON buffer) gated submicron nMOSFETs, while the SiO₂ or SiON control samples show normal short channel effect (SCE) behavior. The possible causes such as inhomogeneous channel doping profile and gate oxide thickness variation near S/D ends have been ruled out. The results indicate that interface trap density that dependents on channel length is the main cause of the RSCE observed here. In addition, oxide charge also plays a role.     

Future directions for the Agency for Health Care Policy and Research

The Agency for Health Care Policy and Research (AHCPR) plays a leading role in health services research. Research efforts to develop practice guidelines, outcomes research, and computer applications have led to improvements in the delivery of care and reduced health care costs. These efforts aid consumers, providers, purchasers, and policy makers in health care decision making. This article cites numerous examples of AHCPR's efforts to increase quality of care and reduce costs.     

1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine as a substrate of cytochrome P450 2D6: allosteric effects of NADPH-cytochrome P450 reductase

1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), a neurotoxin that produces Parkinsonism symptoms in man, has been examined as a substrate of recombinant human cytochrome P450 2D6. When cumene hydroperoxide is used as an oxygen and electron donor, a single product is formed, identified as 4-phenyl-1,2,3,6-tetrahydropyridine. The K(m) for formation of this product (130 microM) is in agreement with the dissociation constants for MPTP binding to the enzyme determined by optical and nuclear magnetic resonance (NMR) spectroscopy. When the reaction is carried out with nicotinamide adenine dinucleotide phosphate (reduced) (NADPH) and recombinant human NADPH-cytochrome P450 reductase, a second product, identified as 1-methyl-4-(4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine, is formed in addition to 4-phenyl-1,2,3,6-tetrahydropyridine. The K(m) values for formation of these two products are 19 microM and 120 microM, respectively. Paramagnetic relaxation experiments have been used to measure distances between the protons of bound MPTP and the heme iron, and these have been used to construct models for the position and orientation of MPTP in the active site. For the cytochrome alone, a single mode of binding was observed, with the N-methyl close to the heme iron in a position appropriate for the observed N-demethylation reaction. In the presence of the reductase, the data were not consistent with a single mode of binding but could be explained by the existence of two alternative orientations of MPTP in the active site. One of these, characterized by a dissociation constant of 150 microM, is essentially identical to that observed in the absence of the reductase. In the second, which has a K(d) of 25 microM, the MPTP is oriented so that the aromatic ring is close to the heme iron, in a position appropriate for p-hydroxylation leading to the formation of the product seen only in the presence of the reductase. In the case of codeine, another substrate for cytochrome P450 2D6, the addition of reductase had no effect on the nature of the product formed, the dissociation constant, or the orientation in the binding site. These observations show that NADPH-cytochrome P450 reductase has an allosteric effect on the active site of cytochrome P450 2D6 that affects the binding of some substrates but not others.