ARXPS-studies ofcˆ-axis textured YBa2Cu3Ox-films

YBa2Cu3Ox sputter deposited cold on MgO grows in O2 annealing epitaxially to a transparent, superconducting film with Tc 80K. The unscraped surfaces of these films are smooth showing XPS lines changing with photoelectron take-off angle. This enhanced data base allows to separate the different chemical compounds (hydroxide, peroxide, carbonate, carboxyle, cuprate, graphite ...) and to obtain their spatial distribution. This yields the compounds, their amount and distribution making up the cinder growing with O2-anneal at internal and external surfaces. The cinder stoichiometry gives insights in the chemistry going on in O2 annealing. Below the cinder the signature ofcˆ-axis oriented YBa2Cu3Ox is identified, showing that a Ba-oxide layer forms the stable surface. This coats insulating CuO2 and Y-oxide layers yielding so an intrinsic dead layer

Helical Contributions Mediate Light-Activated Conformational Change in the LOV2 Domain of <i>Avena sativa</i> Phototropin 1

Algae, plants, bacteria, and fungi contain flavin-binding light-oxygen-voltage (LOV) domains that function as blue light sensors to control cellular responses to light. In the second LOV domain of phototropins, called LOV2 domains, blue light illumination leads to covalent bond formation between protein and flavin that induces the dissociation and unfolding of a C-terminally attached α helix (Jα) and the N-terminal helix (A′α). To date, the majority of studies on these domains have focused on versions that contain truncations in the termini, which creates difficulties when extrapolating to the much larger proteins that contain these domains. Here, we study the influence of deletions and extensions of the A′α helix of the LOV2 domain of Avena sativa phototropin 1 (AsLOV2) on the light-triggered structural response of the protein by Fourier-transform infrared difference spectroscopy. Deletion of the A′α helix abolishes the light-induced unfolding of Jα, whereas extensions of the A′α helix lead to an attenuated structural change of Jα. These results are different from shorter constructs, indicating that the conformational changes in full-length phototropin LOV domains might not be as large as previously assumed, and that the well-characterized full unfolding of the Jα helix in AsLOV2 with short A′α helices may be considered a truncation artifact. It also suggests that the N- and C-terminal helices of phot-LOV2 domains are necessary for allosteric regulation of the phototropin kinase domain and may provide a basis for signal integration of LOV1 and LOV2 domains in phototropins

Distocia en una serpiente ratonera amarilla (iCoelognathus flavolineatus/i, Schlegel 1837) - Relato de caso

La distocia en reptiles, es una patología caracterizada por la dificultad de llevar a cabo el proceso de parto u ovoposición, la literatura es escasa en lo que concierne a distocias en serpientes, por tanto, existen vacíos frente a este tema. Se describe el caso de una serpiente Coelognathus flavolineatus de 10 años de edad que presentaba dificultad en la ovoposición. Fueron evaluados parámetros sanguíneos, radiográficos y ecográficos, así como cultivo bacteriano y antibiograma, con el fin de identificar las posibles causas y complicaciones que desencadenaron el proceso de distocia en la serpiente. En cuanto al tratamiento de la distocia, se realizó una punción aspirativa del huevo a través de la cloaca, extrayéndose su contenido, posteriormente se procedió a extraer los restos y se tomaron hisopados de la mucosa del tracto reproductivo. Las muestras seleccionadas fueron sometidas a cultivo, donde se aislaron cepas de Salmonella del grupo F-67 y Escherichia coli, y en menor proporción cepas de Morganella morganii, Pseudomona aeruginosa, Flavobacterium y Proteus, cuales se atribuyen como agentes infecciosos involucrados en la distocia en la serpiente

BLUF Domain Function Does Not Require a Metastable Radical Intermediate State

BLUF (blue light using flavin) domain proteins are an important family of blue light-sensing proteins which control a wide variety of functions in cells. The primary light-activated step in the BLUF domain is not yet established. A number of experimental and theoretical studies points to a role for photoinduced electron transfer (PET) between a highly conserved tyrosine and the flavin chromophore to form a radical intermediate state. Here we investigate the role of PET in three different BLUF proteins, using ultrafast broadband transient infrared spectroscopy. We characterize and identify infrared active marker modes for excited and ground state species and use them to record photochemical dynamics in the proteins. We also generate mutants which unambiguously show PET and, through isotope labeling of the protein and the chromophore, are able to assign modes characteristic of both flavin and protein radical states. We find that these radical intermediates are not observed in two of the three BLUF domains studied, casting doubt on the importance of the formation of a population of radical intermediates in the BLUF photocycle. Further, unnatural amino acid mutagenesis is used to replace the conserved tyrosine with fluorotyrosines, thus modifying the driving force for the proposed electron transfer reaction; the rate changes observed are also not consistent with a PET mechanism. Thus, while intermediates of PET reactions can be observed in BLUF proteins they are not correlated with photoactivity, suggesting that radical intermediates are not central to their operation. Alternative nonradical pathways including a keto–enol tautomerization induced by electronic excitation of the flavin ring are considered