Angle- and energy-dependent core-level photoelectron energy loss studies in Al and In

Electron energy loss structures of Al and In core-level photoemission spectra, in particular surface and bulk plasmon losses, have been investigated as functions of photon energy (i.e., photoelectron kinetic energy). These studies utilized synchrotron radiation to provide a variable photon source in the ultra-soft X-ray region, thus allowing these loss processes to be studied at photoelectron kinetic energies for which the mean free path of the electrons is minimal. The Al plasmon loss structure was also studied with soft X-ray radiation in an angle-resolved mode, allowing the variation of effective photoelectron sampling depth with different electron take-off (collection) angles. These results for the relative intensity of the bulk and surface plasmons as a function of electron kinetic energy and electron exit angle are in qualitative agreement with the predictions of ?unji? and ?ok?evi?. The core-level binding energies of surface atoms have also been studied with the result that no significant shift has been observed with respect to bulk-atom core levels.     

Analysis of proteins stained by Alexa dyes

Alexa dye staining of proteins is used for the fluorescence microscopy of single particles that are sometimes multimolecular protein complexes. To characterize the staining, post-staining determination must be made of which protein(s) in a complex have been Alexa-stained. The present communication describes the use of sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) for performing this determination. The Alexa-stained proteins are observed directly in gels by illumination with an ultraviolet transilluminator. The test multimolecular particle is bacteriophage T7. The protein capsid of T7 is a multimolecular complex that has both external and internal proteins. SDS-PAGE of Alexa-stained bacteriophage T7 produces fluorescent capsid proteins each of which usually comigrates with an unstained protein. However, one Alexa-induced modification of protein migration was observed by SDS-PAGE. Mass spectrometry shows that the protein with modified migration is the major protein of the outer shell of the T7 capsid. The procedures used are generally applicable. The distribution of Alexa staining among T7 capsid proteins depends on the size of the dye molecule used. The larger the dye molecule is, the greater the preference for external proteins.     

Characterisation of [Cu4S], the catalytic site in nitrous oxide reductase, by EPR spectroscopy

The enzyme nitrous oxide reductase (N(2)OR) has a unique tetranuclear copper centre [Cu(4)S], called Cu(Z), at the catalytic site for the two-electron reduction of N(2)O to N(2). The X- and Q-band EPR spectra have been recorded from two forms of the catalytic site of the enzyme N(2)OR from Paracoccus pantotrophus, namely, a form prepared anaerobically, Cu(Z), that undergoes a one-electron redox cycle and Cu(Z)*, prepared aerobically, which cannot be redox cycled. The spectra of both species are axial with that of Cu(Z) showing a rich hyperfine splitting in the g||-region at X-band. DFT calculations were performed to gain insight into the electronic configuration and ground-state properties of Cu(Z) and to calculate EPR parameters. The results for the oxidation state [Cu(+1)(3)Cu(+2)(1)S](3+) are in good agreement with values obtained from the fitting of experimental spectra, confirming the absolute oxidation state of Cu(Z). The unpaired spin density in this configuration is delocalised over four copper ions, thus, Cu(I) 20.1%, Cu(II) 9.5%, Cu(III) 4.8% and Cu(IV) 9.2%, the mu(4)-sulfide ion and oxygen ligand. The three copper ions carrying the highest spin density plus the sulfide ion lie approximately in the same plane while the fourth copper ion is perpendicular to this plane and carries only 4.8% spin density. It is suggested that the atoms in this plane represent the catalytic core of Cu(Z), allowing electron redistribution within the plane during interaction with the substrate, N(2)O.     

(Arene)tricarbonylchromium complexes synthesized on NaX zeolite: solid-state NMR and DRIFTS studies

Various (arene)tricarbonylchromium complexes were synthesized within the confines of NaX zeolite and studied with diffuse reflectance infrared Fourier transform spectroscopy (DRIFTS) and carbon-13 magic-angle-spinning nuclear magnetic resonance (MAS NMR) spectroscopy. In each case, the surface complex Cr(CO)3(Oz)3 (Oz represents a framework oxygen of the NaX zeolite) was prepared before a particular arene was added. The arenes benzene, toluene, mesitylene, anisole, and aniline all produce hexahapto pi-complexes physisorbed within the zeolite supercage. DRIFTS spectra show three bands in the carbonyl region indicating less than C3v symmetry. The NMR spectra have narrow carbonyl bands near 240 ppm which indicate rapidly reorienting complexes within the zeolite. The (eta 6-benzene)tricarbonylchromium complex is physisorbed at two sites as indicated both by the DRIFTS spectra and by two carbonyl resonances at 242.5 and 239.1 ppm at 300 K. Variable-temperature MAS NMR shows these two resonances coalescing near 360 K with an activation energy of 48 +/- 6 kJ/mol. When the temperature is decreased to 205 K, the high-frequency carbonyl resonance disappears. The 239 ppm resonance is still narrow at 134 K while MAS sidebands show that the resonance from physisorbed benzene is ca. 200 ppm wide. The complex prepared with pyridine gave a broad resonance as indicated by the spinning sidebands in the MAS NMR spectra. The pyridine complex was identified as Cr(CO)3(C5H5N)3.     

Crystal structure determination of 2′-nitro-10-phenylphenothiazine

The structure of the titled compound, 4 , has been solved by x-ray analysis. One of the important structural features of 4 is that the 2′-nitrophenyl group is in the plane bisecting the phenothiazine ring which is in contrast to that of 10-(2′-pyrazyl)phenothiazine of 4′-nitro-10-phenylphenothiazine in which the 10-aryl group is perpendicular to the plane bisecting the phenothiazine ring. The structure of 4 is in agreement with its ¹H and ¹³C nmr data which indicate that resonance interactions between the 2′-nitrophenyl group and the lone pair of electrons on N₁₀ are hindered sterically by the 2′-nitro group.     

Recent progress in carbohydrate separation by high-performance liquid chromatography based on size exclusion

Since the introduction of stationary phases based on microparticulate porous silica and polymeric sorbents, rigid and semi-rigid, size-exclusion chromatography (SEC) has become established as a form of high-performance liquid chromatography. In recent years, there have beeen revolutionary developments in detection systems for high-performance SEC, which have placed the use of the method for the determination of molecular-size and molecular-weight distributions of polymers on a sound theoretical basis andincreased the range of information on molecular characteristics that can be retrieved from SEC data. This review surveys these changes in SEC systems and their application to the separation and molecular-weight distribution analysis of carbohydrates.     

Relaxation effects on auger energies

A hitherto-neglected relaxation-energy effect in the Auger process was found, and an approximate theory for calculating it was developed. The effect ranges from about 6 eV in neon to about 150 eV in fermium. Theoretical KL_IL_I energies show excellent agreement with experiment. The relaxation term is large enough to affect seriously the analysis of unknown Auger spectra. It appears to have very wide application to Auger spectroscopy.