Collectivity in Pb-196,Pb-198 isotopes probed in Coulomb-excitation experiments at REX-ISOLDE

The neutron-deficient Pb-196,Pb-198 isotopes have been studied in Coulomb-excitation experiments employing the Miniball gamma-ray spectrometer and radioactive ion beams from the REX-ISOLDE post-accelerator at CERN. The reduced transition probabilities of the first excited 2(+) states in Pb-196 and Pb-198 nuclei have been measured for the first time. Values of B (E2) = 18.2(-4.1)(+4.8) W. u. and B (E2) = 13.1(-3.5)(+4.9) W. u., were obtained, respectively. The experiment sheds light on the development of collectivity when moving from the regime governed by the generalised seniority scheme to a region, where intruding structures, associated with different deformed shapes, start to come down in energy and approach the spherical ground state.Peer reviewe

Structural basis for the photoconversion of a phytochrome to the activated far-red light-absorbing form

Phytochromes are a collection of bilin-containing photoreceptors that regulate numerous photoresponses in plants and microorganisms through their ability to photointerconvert between a red light-absorbing, ground state Pr and a far-red light-absorbing, photoactivated state Pfr1,2. While the structures of several phytochromes as Pr have been determined3-7, little is known about the structure of Pfr and how it initiates signaling. Here, we describe the three-dimensional solution structure of the bilin-binding domain as Pfr using the cyanobacterial phytochrome from Synechococcus OSB’. Contrary to predictions, light-induced rotation of the A but not the D pyrrole ring is the primary motion of the chromophore during photoconversion. Subsequent rearrangements within the protein then affect intra- and interdomain contact sites within the phytochrome dimer. From our models, we propose that phytochromes act by propagating reversible light-driven conformational changes in the bilin to altered contacts between the adjacent output domains, which in most phytochromes direct differential phosphotransfer

Distinct classes of red/far-red photochemistry within the phytochrome superfamily

Phytochromes are a widespread family of photosensory proteins first discovered in plants, which measure the ratio of red to far-red light to control many aspects of growth and development. Phytochromes interconvert between red-absorbing Pr and far-red-absorbing Pfr states via photoisomerization of a covalently-bound linear tetrapyrrole (bilin) chromophore located in a conserved photosensory core. From recent crystal structures of this core region, it has been inferred that the chromophore structures of Pr and Pfr are conserved in most phytochromes. Using circular dichroism spectroscopy and ab initio calculations, we establish that the Pfr states of the biliverdin-containing bacteriophytochromes DrBphP and PaBphP are structurally dissimilar from those of the phytobilin-containing cyanobacterial phytochrome Cph1. This conclusion is further supported by chromophore substitution experiments using semisynthetic bilin monoamides, which indicate that the propionate side chains perform different functional roles in the 2 classes of phytochromes. We propose that different directions of bilin D-ring rotation account for these distinct classes of red/far-red photochemistry