TY  - JOUR
A1  - Feld, Christian
A1  - Mechie, James
A1  - Hübscher, Christian
A1  - Hall, Jeremy
A1  - Nicolaides, Stelios
A1  - Gurbuz, Cemil
A1  - Bauer, Klaus
A1  - Louden, Keith
A1  - Weber, Michael
T1  - Crustal structure of the eratosthenes seamount, cyprus and S. Turkey from an amphibian wide-angle seismic profile
JF  - Tectonophysics : international journal of geotectonics and the geology and physics of the interior of the earth
N2  - In 2010, project CoCoCo (incipient COntinent-COntinent COllision) recorded a 650 km long amphibian N-S wide-angle seismic profile, extending from the Anatolian plateau across southern Turkey and Cyprus to just south of the Eratosthenes Seamount (ESM). The aim of the project is to reveal the impact of the transition from subduction to continent-continent collision of Africa with Anatolia. Arrival picking, finite-differences ray-tracing and inversion of the offshore and on-offshore data produced a tomographic model across southern Cyprus, the accretionary wedge and the ESM. The main features of this model are (1) crustal P-velocities predominantly lower than 6.5 km/s beneath the ESM, (2) crustal thickness between 28 and 37 km, (3) an upper crustal reflection at 5 km depth beneath the ESM, (4) the likely presence of oceanic crust south of the ESM and a transform margin north of it and (5) a 12 km thick ophiolite sequence on Cyprus. Land shots on Turkey, also recorded on Cyprus, gravity data and geological and previous seismic investigations allow to derive a layered velocity model beneath Anatolia and the northern part of Cyprus. The main features of this model are (1) Moho depths of 38–45 km beneath the Anatolian plateau, (2) an upper and lower crust with large lateral changes in velocity and thickness, (3) a north-dipping subducting plate below Cyprus with a steepening of the dip-angle of the plate at about 45 km depth. Thus, the wide-angle seismic and gravity data provide detailed insights into the 2-D geometry and velocity structures associated with the Cyprus Arc collision zone. Finally, integrated analysis of the geophysics and geology allows a comprehensive interpretation of the crustal structure related to the collision process.
KW  - Controlled source seismology
KW  - Subduction zone processes
KW  - Continental margins: convergent
KW  - Crustal structure
KW  - Europe
KW  - Gravity anomalies and Earth structure
Y1  - 2017
U6  - https://doi.org/10.1016/j.tecto.2017.02.003
SN  - 0040-1951
SN  - 1879-3266
VL  - 700
SP  - 32
EP  - 59
PB  - Elsevier
CY  - Amsterdam
ER  - 
TY  - JOUR
A1  - Hall, James
A1  - Reschke, Stefan
A1  - Cao, Hongnan
A1  - Leimkühler, Silke
A1  - Hille, Russ
T1  - The reductive half-reaction of xanthine dehydrogenase from rhodobacter capsulatus the role of GLU(232) in catalysis
JF  - The journal of biological chemistry
N2  - Background: Kinetic characterization of wild-type xanthine dehydrogenase and variants. Results: Comparison of the pH dependence of both k(red) and k(red)/K-d, as well as k(cat) and k(cat)/K-m. Conclusion: Ionized Glu(232) of wild-type enzyme plays an important role in catalysis by discriminating against the monoanionic form of xanthine. Significance: Examining the contributions of Glu(232) to catalysis is essential for understanding the mechanism of xanthine dehydrogenase.
 The kinetic properties of an E232Q variant of the xanthine dehydrogenase from Rhodobacter capsulatus have been examined to ascertain whether Glu(232) in wild-type enzyme is protonated or unprotonated in the course of catalysis at neutral pH. We find that k(red), the limiting rate constant for reduction at high [xanthine], is significantly compromised in the variant, a result that is inconsistent with Glu(232) being neutral in the active site of the wild-type enzyme. A comparison of the pH dependence of both k(red) and k(red)/K-d from reductive half-reaction experiments between wild-type and enzyme and the E232Q variant suggests that the ionized Glu(232) of wild-type enzyme plays an important role in catalysis by discriminating against the monoanionic form of substrate, effectively increasing the pK(a) of substrate by two pH units and ensuring that at physiological pH the neutral form of substrate predominates in the Michaelis complex. A kinetic isotope study of the wild-type R. capsulatus enzyme indicates that, as previously determined for the bovine and chicken enzymes, product release is principally rate-limiting in catalysis. The disparity in rate constants for the chemical step of the reaction and product release, however, is not as great in the bacterial enzyme as compared with the vertebrate forms. The results indicate that the bacterial and bovine enzymes catalyze the chemical step of the reaction to the same degree and that the faster turnover observed with the bacterial enzyme is due to a faster rate constant for product release than is seen with the vertebrate enzyme.
KW  - Enzyme Kinetics
KW  - Glutamate
KW  - Glutamine
KW  - Isotope Effect
KW  - Ultraviolet-visible Spectroscopy (UV-visible Spectroscopy)
KW  - Xanthine
KW  - Xanthine Dehydrogenase
KW  - Xanthine Oxidase
KW  - pH Dependence
Y1  - 2014
U6  - https://doi.org/10.1074/jbc.M114.603456
SN  - 0021-9258
SN  - 1083-351X
VL  - 289
IS  - 46
SP  - 32121
EP  - 32130
PB  - American Society for Biochemistry and Molecular Biology
CY  - Bethesda
ER  - 
TY  - JOUR
A1  - Radchuk, Viktoriia
A1  - Reed, Thomas
A1  - Teplitsky, Celine
A1  - van de Pol, Martijn
A1  - Charmantier, Anne
A1  - Hassall, Christopher
A1  - Adamik, Peter
A1  - Adriaensen, Frank
A1  - Ahola, Markus P.
A1  - Arcese, Peter
A1  - Miguel Aviles, Jesus
A1  - Balbontin, Javier
A1  - Berg, Karl S.
A1  - Borras, Antoni
A1  - Burthe, Sarah
A1  - Clobert, Jean
A1  - Dehnhard, Nina
A1  - de Lope, Florentino
A1  - Dhondt, Andre A.
A1  - Dingemanse, Niels J.
A1  - Doi, Hideyuki
A1  - Eeva, Tapio
A1  - Fickel, Jörns
A1  - Filella, Iolanda
A1  - Fossoy, Frode
A1  - Goodenough, Anne E.
A1  - Hall, Stephen J. G.
A1  - Hansson, Bengt
A1  - Harris, Michael
A1  - Hasselquist, Dennis
A1  - Hickler, Thomas
A1  - Jasmin Radha, Jasmin
A1  - Kharouba, Heather
A1  - Gabriel Martinez, Juan
A1  - Mihoub, Jean-Baptiste
A1  - Mills, James A.
A1  - Molina-Morales, Mercedes
A1  - Moksnes, Arne
A1  - Ozgul, Arpat
A1  - Parejo, Deseada
A1  - Pilard, Philippe
A1  - Poisbleau, Maud
A1  - Rousset, Francois
A1  - Rödel, Mark-Oliver
A1  - Scott, David
A1  - Carlos Senar, Juan
A1  - Stefanescu, Constanti
A1  - Stokke, Bard G.
A1  - Kusano, Tamotsu
A1  - Tarka, Maja
A1  - Tarwater, Corey E.
A1  - Thonicke, Kirsten
A1  - Thorley, Jack
A1  - Wilting, Andreas
A1  - Tryjanowski, Piotr
A1  - Merila, Juha
A1  - Sheldon, Ben C.
A1  - Moller, Anders Pape
A1  - Matthysen, Erik
A1  - Janzen, Fredric
A1  - Dobson, F. Stephen
A1  - Visser, Marcel E.
A1  - Beissinger, Steven R.
A1  - Courtiol, Alexandre
A1  - Kramer-Schadt, Stephanie
T1  - Adaptive responses of animals to climate change are most likely insufficient
JF  - Nature Communications
N2  - Biological responses to climate change have been widely documented across taxa and regions, but it remains unclear whether species are maintaining a good match between phenotype and environment, i.e. whether observed trait changes are adaptive. Here we reviewed 10,090 abstracts and extracted data from 71 studies reported in 58 relevant publications, to assess quantitatively whether phenotypic trait changes associated with climate change are adaptive in animals. A meta-analysis focussing on birds, the taxon best represented in our dataset, suggests that global warming has not systematically affected morphological traits, but has advanced phenological traits. We demonstrate that these advances are adaptive for some species, but imperfect as evidenced by the observed consistent selection for earlier timing. Application of a theoretical model indicates that the evolutionary load imposed by incomplete adaptive responses to ongoing climate change may already be threatening the persistence of species.
Y1  - 2019
U6  - https://doi.org/10.1038/s41467-019-10924-4
SN  - 2041-1723
VL  - 10
PB  - Nature Publ. Group
CY  - London
ER  -