The current-carrying corner inherent to trench isolation

It is shown how the characteristics of the corner MOSFET inherent to trench isolation can be extracted from hardware measurements and how the corner device must be taken into account when extracting MOSFET channel characteristics. For NFETs it is found that the corner's threshold voltage, substrate sensitivity, and sensitivity to well doping are all smaller than the channel's. The results imply that for low-standby-power logic applications requiring high performance, it may become necessary to locally control the well doping at the corner. However, the corner's reduced substrate sensitivity and width independence can provide a significant advantage in a DRAM cell     

Anomalous narrow channel effect in trench-isolated buried-channelp-MOSFET's

An anomalous threshold voltage dependence on channel width measured on 0.25 μm groundrule trench-isolated buried-channel p-MOSFET's is reported here. As the channel width is reduced, the magnitude of the threshold voltage first decreases before the onset of the expected sharp rise in Vt for widths narrower than 0.4 μm. Modeling shows that a “boron puddle” is created near the trench bounded edge as a result of transient enhanced diffusion (TED) during the gate oxidation step. TED is governed by interstitials produced by a deep phosphorus implant, used for latchup suppression, diffusing towards the trench sidewall and top surface of the device. The presence of the “boron puddle” imposes a penalty on the off-current of narrow devices. A solution for minimizing the “boron puddle” is demonstrated with simulations, confirmed by measurements     

Spectroscopic characterization of recombinant pea cytosolic ascorbate peroxidase: similarities and differences with cytochrome c peroxidase

Recombinant pea cytosolic ascorbate peroxidase (APX) has been characterized by resonance Raman (RR) and electronic absorption spectroscopies. The ferric and ferrous forms together with the complexes with fluoride and imidazole have been studied and compared with the corresponding spectra of cytochrome c peroxidase (CCP). Ferric APX at neutral pH is a mixture of 6- and 5-coordinate high-spin and 6-c low-spin hemes, the latter two species being dominant. The results suggest that the low-spin form derives from a water/hydroxo ligand bound to the heme iron and not from a strong internal ligand as observed in CCP at alkaline pH. Two Fe-Im stretching modes are identified, as in CCP, but the RR frequencies confirm a weaker His163-Asp208 hydrogen bond than in CCP, as suggested on the basis of the X-ray structure [Patterson, W. R., and Poulos, T. L. (1995) Biochemistry 34, 4331-4341]. The data show that CCP and APX have markedly different orientations of the vinyl substituents on the heme chromophore resulting from different steric constraints exerted by the protein matrix.     

Identification of two electron-transfer sites in ascorbate peroxidase using chemical modification, enzyme kinetics, and crystallography

Chemical and mutagenic modification combined with X-ray crystallography has been used to probe the ascorbate binding site in ascorbate peroxidase (APX). Chemical modification of the single Cys residue in APX with Ellman's reagent (DTNB) blocks the ability of APX to oxidize ascorbate but not other small aromatic phenolic substrates. DTNB-modified APX (APX-TNB) exhibits only 1.3% wild-type activity when ascorbate is used as the substrate but full activity when aromatic substrates, guaiacol or pyrogallol, are used. Stopped-flow studies show that APX-TNB reacts normally with peroxide to give compound I but that the rates of reduction of both compounds I and II by ascorbate are dramatically slowed. Conversion of Cys32 to Ser leads to approximately 70% drop in ascorbate peroxidase activity with no effect on guaiacol peroxidase activity. These results indicate that uncharged aromatic substrates and the anionic ascorbate molecule interact with different sites on APX. The 2.0 A X-ray crystal structure of APX-TNB shows clear electron density for the TNB group covalently attached to Cys32 in all four molecules of the asymmetric unit, indicating complete and specific modification. It appears that the ascorbate site is blocked by DTNB modification which is well removed from the exposed delta-heme edge where aromatic substrates are thought to bind. This is the first experimental evidence indicating that ascorbate oxidation does not occur at the exposed heme edge but at an alternate binding site in the vicinity of Cys32 near Arg172 and the heme propionates.