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The regeneration cycle of expensive cofactor, NAD(P)H, is of paramount importance for the bio-catalyzed redox reactions. Here a ZrO2supported bimetallic nanocatalyst of gold-palladium (Au-Pd/ZrO2) was prepared to catalyze the regeneration of NAD(P)H without using electron mediators and extra energy input. Over 98% of regeneration efficiency can be achieved catlyzed by Au-Pd/ZrO2using TEOA as the electron donor. Mechanism study showed that the regeneration of NAD(P)H took place through a two-step process: Au-Pd/ZrO2nanocatalyst first catalyzed the oxidation of triethanolamine (TEOA) to glycolaldehyde (GA), then the generated GA induced the non-catalytic reducing of NAD(P)+to NAD(P)H under an alkaline environment maintained by TEOA. This two-step mechanism enables the decoupling of the regeneration of NAD(P)H in space and time into a catalytic oxidation and non-catalytic reducing cascade process which has been further verified using a variety of electron donors. The application significance of this procedure is further demonstrated both by the favorable stability of Au-Pd/ZrO2nanocatalyst in 5 successive cycles preserving over 90% of its original activity, and by the excellent performance of the regenerated NADH as the cofactor in the catalytic hydrogenation of acetaldehyde using an ethanol dehydrogenase.

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The interest in Robertsonian fusion chromosomes (Rb fusions), sometimes referred to as Robertsonian translocations, derives from their impact on mammalian karyotype evolution, as well from their influence on fertility and disease. The formation of a Rb chromosome necessitates the occurrence of double strand breaks in the pericentromeric regions of two chromosomes in the satellite DNA (satDNA) sequences. Here, we report on the fine-scale molecular analysis of the centromeric satDNA families in the Rb(1;29) translocation of domestic cattle and six antelope species of the subfamily Bovinae. We do so from two perspectives: its occurrence as a chromosomal abnormality in cattle and, secondly, as a fixed evolutionarily rearrangement in spiral-horned antelope (Tragelaphini). By analysing the reorganization of satDNAs in the centromeric regions of translocated chromosomes, we show that Rb fusions are multistep, complex rearrangements which entail the precise elimination and reorganization of specific (peri)centromeric satDNA sequences. Importantly, these structural changes do not influence the centromeric activity of the satellite DNAs that provide segregation stability to the translocated chromosome. Our results suggest a common mechanism for Rb fusions in these bovids and, more widely, for mammals in general.

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This paper presents a review of our original results obtained during the last decade. These results have been found theoretically for classical mass-action-law models of chemical kinetics and justified experimentally. In contrast with the traditional invariances, they relate to a special battery of kinetic experiments, not a single experiment. Two types of invariances are distinguished and described in detail: thermodynamic invariants, i.e., special combinations of kinetic dependences that yield the equilibrium constants, or simple functions of the equilibrium constants; and "mixed" kinetico-thermodynamic invariances, functions both of equilibrium constants and non-thermodynamic ratios of kinetic coefficients.

RESUMEN

Protein-dense liquid clusters are regions of high protein concentration that have been observed in solutions of several proteins. The typical cluster size varies from several tens to several hundreds of nanometres and their volume fraction remains below 10(-3) of the solution. According to the two-step mechanism of nucleation, the protein-rich clusters serve as locations for and precursors to the nucleation of protein crystals. While the two-step mechanism explained several unusual features of protein crystal nucleation kinetics, a direct observation of its validity for protein crystals has been lacking. Here, two independent observations of crystal nucleation with the proteins lysozyme and glucose isomerase are discussed. Firstly, the evolutions of the protein-rich clusters and nucleating crystals were characterized simultaneously by dynamic light scattering (DLS) and confocal depolarized dynamic light scattering (cDDLS), respectively. It is demonstrated that protein crystals appear following a significant delay after cluster formation. The cDDLS correlation functions follow a Gaussian decay, indicative of nondiffusive motion. A possible explanation is that the crystals are contained inside large clusters and are driven by the elasticity of the cluster surface. Secondly, depolarized oblique illumination dark-field microscopy reveals the evolution from liquid clusters without crystals to newly nucleated crystals contained in the clusters to grown crystals freely diffusing in the solution. Collectively, the observations indicate that the protein-rich clusters in lysozyme and glucose isomerase solutions are locations for crystal nucleation.

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