Jahn-teller dynamics in charge-ordered manganites from raman spectroscopy

The Raman spectra of the charge-ordered manganite Pr0.65Ca0.35MnO3 were studied as functions of temperature and excitation energy and compared to magnetic moment and electrical conductivity behaviors. Both the charge ordering ( T(co) approximately 225 K) and the antiferromagnetic transitions ( T(N) approximately 175 K) affect the spectral shape and intensity, indicating strong charge-lattice and spin-lattice couplings. Below T(co) a transition from dynamic Jahn-Teller distortions to a collective static distortion takes place. A change of the spectra is observed on increasing the excitation energy above 2.5 eV and it is attributed to a resonant polaron excitation.     

Radiation zeros and gravity

The existence of spin independent zeros in every tree approximated radiation amplitude in gauge theories is examined when quantum gravity is included. Using a direct evaluation of the relevant transition amplitudes a series of results is proven. They are mostly negative showing that there is no general mechanism of cancellation when quantum gravity is present. The question of gravitational radiation zeros is also addressed and their absence is inferred.     

Synthesis,stereochemistry and conformational properties of diastereomeric cyclic dipeptides containing tetrahydro-1,4-thiazine-3,5-dicarboxylic acid

The synthesis of linear dipeptides containing N-protected L-phenylalanine and (3R-cis)-tetrahydro-1,4-thiazine-3,5-dicarboxylic acid dialkyl diester residues is described. N-Deprotection of these dipeptides by hydrogenolysis on palladium afforded directly a mixture of cis and trans dioxopiperazines. The stereochemistry and the solution conformational properties of the cyclic dipeptides are determined.     

The reactivity of 2,3-diaminopyridine toward alkyl chloroformates and dicarbonates

The reaction of 2,3-diaminopyridine (DAP) with alkyl chloroformates and dialkyl dicarbonates is affected by the nature of the acylating agent and the acylation conditions. Mono and dicarbamates of DAP were obtained using chloroformates, while the formation of alkoxycarbonyl derivatives of imidazo[4,5-b]pyridin-2-one was observed when the reaction with dicarbonates was performed at room temperature in THF-pyridine. Our procedure for the synthesis of imidazopyridin-2-ones represents an improvement over the previous methods which require rather severe conditions. The revised structure for a monoacetyl derivative of the above bicyclic system is also reported.     

Design of a new mimochrome with unique topology

Peptide-based metalloprotein models represent useful systems to help understand how metalloproteins can support different functions, by the use of similar metal ion cofactors. In order to shed light on the role of the protein matrix in modulating the heme properties, we developed new models: mimochromes. They are pseudo-C(2) symmetric systems, composed of two helical peptides covalently linked to the deuteroporphyrin. The use of C(2) symmetry is particularly advantageous, because it simplifies the design, synthesis and characterization. However, it leaves the problem of possible diastereomeric forms. In the cobalt complex of the first derivative, mimochrome I, Lambda and Delta isomers were indeed experimentally observed. All the insights derived from the Co(III)-mimochrome I structure were used to obtain a re-designed molecule, mimochrome IV. The spectroscopic characterization of the iron and cobalt derivatives suggested the presence of the Lambda isomer as unique species. The NMR solution structure of the diamagnetic Co(III)-mimochrome IV confirmed the ability of the molecule to adopt a unique topology, and revealed the peptide chains to be in helical conformation, as designed. The insertion of intramolecular, inter-chain interactions was successful in favoring the formation of one of the two possible diastereomers. The stereochemically stable structure of mimochrome IV provides an attractive model for modulating the redox potential of the heme, by simple changing the peptide chain composition around the heme.