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