Pseudopotential Approaches to Ca, Sr and Ba Hybrides. Why are some Alkaline Earth MX2_2 Compounds Bent?

Quasirelativistic and nonrelativistic lo-valence-electronp seudopotentialsf or Ca, Sr, and Ba are presented. Results of calculations with 6s6p5d basis sets for MH, MH$^+$ , and MH$_2$, are compared with all-electron and 2-valence-electron pseudopotential calculations with and , without core-polarization potentials. The lo-valence-electron pseudopotential approach agrees well with all-electron calculations. It circumvents problems for the 2-valence-electron pseudopotentials arising from an incomplete separation of valence and subvalence shells in polar molecular systems due to strongly contracted occupied (n - 1 )-d orbitals. All higherlevel calculations show SrH$_2$ and BaII$_2$, to be bent with angles of - 140° and 120°, respectively, while CaH$_2$ is linear with a flat potential-energy surface for the bending motion. The use of a core-polarization potential together with the 2-valence-electronp seudopotentiala pproach allows an investigation of the relative importance of core-polarization vs direct d-orbital bonding participation as reasons for the bent structures. The calculations strongly suggest that both contribute to the bending in SrH$_2$ and BaII$_2$. Even at the Hartree-Fock level of theory lovalence- electronp seudopotentialc alculations given reasonablea nglesw hen the potentialenergy surface is not exceedingly flat, and only moderately contracted basis sets including both compact d functions and diffuse p functions are used. The effect of core-valence correlation and the importance off functions also are discussed

The Heme Protein P450 from Adrenal Cortex: Its Reactivities in Ferric and Ferrous Forms

In the course of this reaction cycle the heme protein undergoes a series of changes of its coordination around the Fe (on reduction to its »unliganded~ Fe2+ state, on binding of the 0 2 molecule, and upon introduction of the second reducing equivalent, as the heme protein returns to its original Fe3+ state}. Steroid substrates, inhibitors, and a variety of agents bind to the heme protein P450(Fe3+), isolated in a S = 1/2 form from bovine adrenal glands, with high affinities at sites near the heme group, but do not as a rule enter the coordination sphere of the Fe. This leads to perturbations of the electronic structure which can be followed by spectroscopic techniques (optical absorption, EPR spectroscopy) in combination with suitable chemical methods. Direct replacement of a ligand can also be achieved. The ferrous heme protein P450(Fe2+), in its unliganded and liganded forms, was also investigated. P450(Fe2•) combines readily with small ligands such as 0 2 (418 nm), CO (448 nm), and nitric oxide. Larger lipophilic molecules (e. g. pyridine derivatives, other heterocyclic compounds, haloalkanes, or hydroperoxides) also bind readily to P450(Fe2+), often with high affinities. They tend to enter the coordination sphere of the Fe and form stable complexes often with distinct optical absorption (440-470 nm); additional unspecific binding is frequently observed. Representative examples of the results for the various cases of interactions are presented and are discussed in relation to a hypothetical structure of P450(Fe3• ), S = 1/2, as a protoheme IX complex, with a thiol-group and a N-containing group as axial ligands; the observations are further related to the required changes in coordination in the course of the hydroxylation reaction

The Heme Protein P450 from Adrenal Cortex: Its Reactivities in Ferric and Ferrous Forms

In the course of this reaction cycle the heme protein undergoes a series of changes of its coordination around the Fe (on reduction to its »unliganded~ Fe2+ state, on binding of the 0 2 molecule, and upon introduction of the second reducing equivalent, as the heme protein returns to its original Fe3+ state}. Steroid substrates, inhibitors, and a variety of agents bind to the heme protein P450(Fe3+), isolated in a S = 1/2 form from bovine adrenal glands, with high affinities at sites near the heme group, but do not as a rule enter the coordination sphere of the Fe. This leads to perturbations of the electronic structure which can be followed by spectroscopic techniques (optical absorption, EPR spectroscopy) in combination with suitable chemical methods. Direct replacement of a ligand can also be achieved. The ferrous heme protein P450(Fe2+), in its unliganded and liganded forms, was also investigated. P450(Fe2•) combines readily with small ligands such as 0 2 (418 nm), CO (448 nm), and nitric oxide. Larger lipophilic molecules (e. g. pyridine derivatives, other heterocyclic compounds, haloalkanes, or hydroperoxides) also bind readily to P450(Fe2+), often with high affinities. They tend to enter the coordination sphere of the Fe and form stable complexes often with distinct optical absorption (440-470 nm); additional unspecific binding is frequently observed. Representative examples of the results for the various cases of interactions are presented and are discussed in relation to a hypothetical structure of P450(Fe3• ), S = 1/2, as a protoheme IX complex, with a thiol-group and a N-containing group as axial ligands; the observations are further related to the required changes in coordination in the course of the hydroxylation reaction

Biogenesis of the mitochondrial phosphate carrier

The mitochondrial phosphate carrier (PiC) is a member of the family of inner-membrane carrier proteins which are generally synthesized without a cleavable presequence. Surprisingly, the cDNA sequences of bovine and rat PiC suggested the existence of an amino-terminal extension sequence in the precursor of PiC. By expressing PiC in vitro, we found that PiC is indeed synthesized as a larger precursor. This precursor was imported and proteolytically processed by mitochondria, whereby the correct amino-terminus of the mature protein was generated. Import of PiC showed the characteristics of mitochondrial protein uptake, such as dependence on ATP and a membrane potential and involvement of contact sites between mitochondrial outer and inner membranes. The precursor imported in vitro was correctly assembled into the functional form, demonstrating that the authentic import and assembly pathway of PiC was reconstituted when starting with the presequence-carrying precursor. These results are discussed in connection with the recently postulated role of PiC as an import receptor located in the outer membrane

Structure of Africa\u27s Southernmost Coral Communities

The structure of Africa\u27s southernmost coral communities, which grow on submerged fossil dune and beachrock systems and do not form true coral reefs, was quantitatively investigated by means of line transects and phototransects. None of the typical geomorphological reef-zones such as lagoons, reef crests or reef slopes were developed. A uniform community structure, differentiated only into two major community-types with three subcommunities, was found, Shallow reefs were dominated by alcyonaceans and differed from scleractinian dominated deep reefs. A high proportion of alcyonaceans was found in shallow communities (40–60%). Subcommunities, which were found on most reefs, were an alcyonacean dominated reef-top community in areas of low sedimentation, dominated by the genera Sinularia and Lobophytum, and a scleractinian dominated gully community (predominantly Montipora and Faviidae), in areas of high sedimentation. A deep sponge-dominated subcommunity existed on the deepest outcrops. The lower limit for most coral growth was between 35 and 40 m

MeSH term explosion and author rank improve expert recommendations

Abstrac

Advanced design and characterization methodologies for memory-aware CMOS power-amplifier implementation

This paper reports on an effective root-cause analysis method of memory effects in power amplifiers, as well as introduces compensation techniques on a circuit design level. Despite conventional memory-effect approaches, the discussed method uses a two-tone scan over a wide operation and modulation range. This enables an in-depth study of physical causes and helps to implement compensation techniques at design stage. On the one hand, this circuit investigation is optimized using an automated SystemC model parametrized with real device and measurement values. Hence, computation time is widely reduced which shortens design cycles. On the other hand, the implementation of the derived circuit compensation means will reduce the complexity of digital pre-distortion due to a reduced memory-effect induced AM/AM and AM/PM hysteresis. The approach is demonstrated on a 65 nm CMOS power amplifier with an OIP1 of 27 dBm and a PAE of over 30 % using WCDMA and LTE signals. In fact, mismatch could be reduced by more than 8 %