TY  - JOUR
A1  - Wuttke, Matthias
A1  - Li, Yong
A1  - Li, Man
A1  - Sieber, Karsten B.
A1  - Feitosa, Mary F.
A1  - Gorski, Mathias
A1  - Tin, Adrienne
A1  - Wang, Lihua
A1  - Chu, Audrey Y.
A1  - Hoppmann, Anselm
A1  - Kirsten, Holger
A1  - Giri, Ayush
A1  - Chai, Jin-Fang
A1  - Sveinbjornsson, Gardar
A1  - Tayo, Bamidele O.
A1  - Nutile, Teresa
A1  - Fuchsberger, Christian
A1  - Marten, Jonathan
A1  - Cocca, Massimiliano
A1  - Ghasemi, Sahar
A1  - Xu, Yizhe
A1  - Horn, Katrin
A1  - Noce, Damia
A1  - Van der Most, Peter J.
A1  - Sedaghat, Sanaz
A1  - Yu, Zhi
A1  - Akiyama, Masato
A1  - Afaq, Saima
A1  - Ahluwalia, Tarunveer Singh
A1  - Almgren, Peter
A1  - Amin, Najaf
A1  - Arnlov, Johan
A1  - Bakker, Stephan J. L.
A1  - Bansal, Nisha
A1  - Baptista, Daniela
A1  - Bergmann, Sven
A1  - Biggs, Mary L.
A1  - Biino, Ginevra
A1  - Boehnke, Michael
A1  - Boerwinkle, Eric
A1  - Boissel, Mathilde
A1  - Böttinger, Erwin
A1  - Boutin, Thibaud S.
A1  - Brenner, Hermann
A1  - Brumat, Marco
A1  - Burkhardt, Ralph
A1  - Butterworth, Adam S.
A1  - Campana, Eric
A1  - Campbell, Archie
A1  - Campbell, Harry
A1  - Canouil, Mickael
A1  - Carroll, Robert J.
A1  - Catamo, Eulalia
A1  - Chambers, John C.
A1  - Chee, Miao-Ling
A1  - Chee, Miao-Li
A1  - Chen, Xu
A1  - Cheng, Ching-Yu
A1  - Cheng, Yurong
A1  - Christensen, Kaare
A1  - Cifkova, Renata
A1  - Ciullo, Marina
A1  - Concas, Maria Pina
A1  - Cook, James P.
A1  - Coresh, Josef
A1  - Corre, Tanguy
A1  - Sala, Cinzia Felicita
A1  - Cusi, Daniele
A1  - Danesh, John
A1  - Daw, E. Warwick
A1  - De Borst, Martin H.
A1  - De Grandi, Alessandro
A1  - De Mutsert, Renee
A1  - De Vries, Aiko P. J.
A1  - Degenhardt, Frauke
A1  - Delgado, Graciela
A1  - Demirkan, Ayse
A1  - Di Angelantonio, Emanuele
A1  - Dittrich, Katalin
A1  - Divers, Jasmin
A1  - Dorajoo, Rajkumar
A1  - Eckardt, Kai-Uwe
A1  - Ehret, Georg
A1  - Elliott, Paul
A1  - Endlich, Karlhans
A1  - Evans, Michele K.
A1  - Felix, Janine F.
A1  - Foo, Valencia Hui Xian
A1  - Franco, Oscar H.
A1  - Franke, Andre
A1  - Freedman, Barry I.
A1  - Freitag-Wolf, Sandra
A1  - Friedlander, Yechiel
A1  - Froguel, Philippe
A1  - Gansevoort, Ron T.
A1  - Gao, He
A1  - Gasparini, Paolo
A1  - Gaziano, J. Michael
A1  - Giedraitis, Vilmantas
A1  - Gieger, Christian
A1  - Girotto, Giorgia
A1  - Giulianini, Franco
A1  - Gogele, Martin
A1  - Gordon, Scott D.
A1  - Gudbjartsson, Daniel F.
A1  - Gudnason, Vilmundur
A1  - Haller, Toomas
A1  - Hamet, Pavel
A1  - Harris, Tamara B.
A1  - Hartman, Catharina A.
A1  - Hayward, Caroline
A1  - Hellwege, Jacklyn N.
A1  - Heng, Chew-Kiat
A1  - Hicks, Andrew A.
A1  - Hofer, Edith
A1  - Huang, Wei
A1  - Hutri-Kahonen, Nina
A1  - Hwang, Shih-Jen
A1  - Ikram, M. Arfan
A1  - Indridason, Olafur S.
A1  - Ingelsson, Erik
A1  - Ising, Marcus
A1  - Jaddoe, Vincent W. V.
A1  - Jakobsdottir, Johanna
A1  - Jonas, Jost B.
A1  - Joshi, Peter K.
A1  - Josyula, Navya Shilpa
A1  - Jung, Bettina
A1  - Kahonen, Mika
A1  - Kamatani, Yoichiro
A1  - Kammerer, Candace M.
A1  - Kanai, Masahiro
A1  - Kastarinen, Mika
A1  - Kerr, Shona M.
A1  - Khor, Chiea-Chuen
A1  - Kiess, Wieland
A1  - Kleber, Marcus E.
A1  - Koenig, Wolfgang
A1  - Kooner, Jaspal S.
A1  - Korner, Antje
A1  - Kovacs, Peter
A1  - Kraja, Aldi T.
A1  - Krajcoviechova, Alena
A1  - Kramer, Holly
A1  - Kramer, Bernhard K.
A1  - Kronenberg, Florian
A1  - Kubo, Michiaki
A1  - Kuhnel, Brigitte
A1  - Kuokkanen, Mikko
A1  - Kuusisto, Johanna
A1  - La Bianca, Martina
A1  - Laakso, Markku
A1  - Lange, Leslie A.
A1  - Langefeld, Carl D.
A1  - Lee, Jeannette Jen-Mai
A1  - Lehne, Benjamin
A1  - Lehtimaki, Terho
A1  - Lieb, Wolfgang
A1  - Lim, Su-Chi
A1  - Lind, Lars
A1  - Lindgren, Cecilia M.
A1  - Liu, Jun
A1  - Liu, Jianjun
A1  - Loeffler, Markus
A1  - Loos, Ruth J. F.
A1  - Lucae, Susanne
A1  - Lukas, Mary Ann
A1  - Lyytikainen, Leo-Pekka
A1  - Magi, Reedik
A1  - Magnusson, Patrik K. E.
A1  - Mahajan, Anubha
A1  - Martin, Nicholas G.
A1  - Martins, Jade
A1  - Marz, Winfried
A1  - Mascalzoni, Deborah
A1  - Matsuda, Koichi
A1  - Meisinger, Christa
A1  - Meitinger, Thomas
A1  - Melander, Olle
A1  - Metspalu, Andres
A1  - Mikaelsdottir, Evgenia K.
A1  - Milaneschi, Yuri
A1  - Miliku, Kozeta
A1  - Mishra, Pashupati P.
A1  - Program, V. A. Million Veteran
A1  - Mohlke, Karen L.
A1  - Mononen, Nina
A1  - Montgomery, Grant W.
A1  - Mook-Kanamori, Dennis O.
A1  - Mychaleckyj, Josyf C.
A1  - Nadkarni, Girish N.
A1  - Nalls, Mike A.
A1  - Nauck, Matthias
A1  - Nikus, Kjell
A1  - Ning, Boting
A1  - Nolte, Ilja M.
A1  - Noordam, Raymond
A1  - Olafsson, Isleifur
A1  - Oldehinkel, Albertine J.
A1  - Orho-Melander, Marju
A1  - Ouwehand, Willem H.
A1  - Padmanabhan, Sandosh
A1  - Palmer, Nicholette D.
A1  - Palsson, Runolfur
A1  - Penninx, Brenda W. J. H.
A1  - Perls, Thomas
A1  - Perola, Markus
A1  - Pirastu, Mario
A1  - Pirastu, Nicola
A1  - Pistis, Giorgio
A1  - Podgornaia, Anna I.
A1  - Polasek, Ozren
A1  - Ponte, Belen
A1  - Porteous, David J.
A1  - Poulain, Tanja
A1  - Pramstaller, Peter P.
A1  - Preuss, Michael H.
A1  - Prins, Bram P.
A1  - Province, Michael A.
A1  - Rabelink, Ton J.
A1  - Raffield, Laura M.
A1  - Raitakari, Olli T.
A1  - Reilly, Dermot F.
A1  - Rettig, Rainer
A1  - Rheinberger, Myriam
A1  - Rice, Kenneth M.
A1  - Ridker, Paul M.
A1  - Rivadeneira, Fernando
A1  - Rizzi, Federica
A1  - Roberts, David J.
A1  - Robino, Antonietta
A1  - Rossing, Peter
A1  - Rudan, Igor
A1  - Rueedi, Rico
A1  - Ruggiero, Daniela
A1  - Ryan, Kathleen A.
A1  - Saba, Yasaman
A1  - Sabanayagam, Charumathi
A1  - Salomaa, Veikko
A1  - Salvi, Erika
A1  - Saum, Kai-Uwe
A1  - Schmidt, Helena
A1  - Schmidt, Reinhold
A1  - Ben Schottker, 
A1  - Schulz, Christina-Alexandra
A1  - Schupf, Nicole
A1  - Shaffer, Christian M.
A1  - Shi, Yuan
A1  - Smith, Albert V.
A1  - Smith, Blair H.
A1  - Soranzo, Nicole
A1  - Spracklen, Cassandra N.
A1  - Strauch, Konstantin
A1  - Stringham, Heather M.
A1  - Stumvoll, Michael
A1  - Svensson, Per O.
A1  - Szymczak, Silke
A1  - Tai, E-Shyong
A1  - Tajuddin, Salman M.
A1  - Tan, Nicholas Y. Q.
A1  - Taylor, Kent D.
A1  - Teren, Andrej
A1  - Tham, Yih-Chung
A1  - Thiery, Joachim
A1  - Thio, Chris H. L.
A1  - Thomsen, Hauke
A1  - Thorleifsson, Gudmar
A1  - Toniolo, Daniela
A1  - Tonjes, Anke
A1  - Tremblay, Johanne
A1  - Tzoulaki, Ioanna
A1  - Uitterlinden, Andre G.
A1  - Vaccargiu, Simona
A1  - Van Dam, Rob M.
A1  - Van der Harst, Pim
A1  - Van Duijn, Cornelia M.
A1  - Edward, Digna R. Velez
A1  - Verweij, Niek
A1  - Vogelezang, Suzanne
A1  - Volker, Uwe
A1  - Vollenweider, Peter
A1  - Waeber, Gerard
A1  - Waldenberger, Melanie
A1  - Wallentin, Lars
A1  - Wang, Ya Xing
A1  - Wang, Chaolong
A1  - Waterworth, Dawn M.
A1  - Bin Wei, Wen
A1  - White, Harvey
A1  - Whitfield, John B.
A1  - Wild, Sarah H.
A1  - Wilson, James F.
A1  - Wojczynski, Mary K.
A1  - Wong, Charlene
A1  - Wong, Tien-Yin
A1  - Xu, Liang
A1  - Yang, Qiong
A1  - Yasuda, Masayuki
A1  - Yerges-Armstrong, Laura M.
A1  - Zhang, Weihua
A1  - Zonderman, Alan B.
A1  - Rotter, Jerome I.
A1  - Bochud, Murielle
A1  - Psaty, Bruce M.
A1  - Vitart, Veronique
A1  - Wilson, James G.
A1  - Dehghan, Abbas
A1  - Parsa, Afshin
A1  - Chasman, Daniel I.
A1  - Ho, Kevin
A1  - Morris, Andrew P.
A1  - Devuyst, Olivier
A1  - Akilesh, Shreeram
A1  - Pendergrass, Sarah A.
A1  - Sim, Xueling
A1  - Boger, Carsten A.
A1  - Okada, Yukinori
A1  - Edwards, Todd L.
A1  - Snieder, Harold
A1  - Stefansson, Kari
A1  - Hung, Adriana M.
A1  - Heid, Iris M.
A1  - Scholz, Markus
A1  - Teumer, Alexander
A1  - Kottgen, Anna
A1  - Pattaro, Cristian
T1  - A catalog of genetic loci associated with kidney function from analyses of a million individuals
JF  - Nature genetics
N2  - Chronic kidney disease (CKD) is responsible for a public health burden with multi-systemic complications. Through transancestry meta-analysis of genome-wide association studies of estimated glomerular filtration rate (eGFR) and independent replication (n = 1,046,070), we identified 264 associated loci (166 new). Of these,147 were likely to be relevant for kidney function on the basis of associations with the alternative kidney function marker blood urea nitrogen (n = 416,178). Pathway and enrichment analyses, including mouse models with renal phenotypes, support the kidney as the main target organ. A genetic risk score for lower eGFR was associated with clinically diagnosed CKD in 452,264 independent individuals. Colocalization analyses of associations with eGFR among 783,978 European-ancestry individuals and gene expression across 46 human tissues, including tubulo-interstitial and glomerular kidney compartments, identified 17 genes differentially expressed in kidney. Fine-mapping highlighted missense driver variants in 11 genes and kidney-specific regulatory variants. These results provide a comprehensive priority list of molecular targets for translational research.
Y1  - 2019
U6  - https://doi.org/10.1038/s41588-019-0407-x
SN  - 1061-4036
SN  - 1546-1718
VL  - 51
IS  - 6
SP  - 957
EP  - +
PB  - Nature Publ. Group
CY  - New York
ER  - 
TY  - JOUR
A1  - Kubin, Markus
A1  - Guo, Meiyuan
A1  - Kroll, Thomas
A1  - Loechel, Heike
A1  - Kallman, Erik
A1  - Baker, Michael L.
A1  - Mitzner, Rolf
A1  - Gul, Sheraz
A1  - Kern, Jan
A1  - Föhlisch, Alexander
A1  - Erko, Alexei
A1  - Bergmann, Uwe
A1  - Yachandra, Vittal
A1  - Yano, Junko
A1  - Lundberg, Marcus
A1  - Wernet, Philippe
T1  - Probing the oxidation state of transition metal complexes
BT  - a case study on how charge and spin densities determine Mn L-edge X-ray absorption energies
JF  - Chemical science
N2  - Transition metals in inorganic systems and metalloproteins can occur in different oxidation states, which makes them ideal redox-active catalysts. To gain a mechanistic understanding of the catalytic reactions, knowledge of the oxidation state of the active metals, ideally in operando, is therefore critical. L-edge X-ray absorption spectroscopy (XAS) is a powerful technique that is frequently used to infer the oxidation state via a distinct blue shift of L-edge absorption energies with increasing oxidation state. A unified description accounting for quantum-chemical notions whereupon oxidation does not occur locally on the metal but on the whole molecule and the basic understanding that L-edge XAS probes the electronic structure locally at the metal has been missing to date. Here we quantify how charge and spin densities change at the metal and throughout the molecule for both redox and core-excitation processes. We explain the origin of the L-edge XAS shift between the high-spin complexes Mn-II(acac)(2) and Mn-III(acac)(3) as representative model systems and use ab initio theory to uncouple effects of oxidation-state changes from geometric effects. The shift reflects an increased electron affinity of Mn-III in the core-excited states compared to the ground state due to a contraction of the Mn 3d shell upon core-excitation with accompanied changes in the classical Coulomb interactions. This new picture quantifies how the metal-centered core hole probes changes in formal oxidation state and encloses and substantiates earlier explanations. The approach is broadly applicable to mechanistic studies of redox-catalytic reactions in molecular systems where charge and spin localization/delocalization determine reaction pathways.
Y1  - 2018
U6  - https://doi.org/10.1039/c8sc00550h
SN  - 2041-6520
SN  - 2041-6539
VL  - 9
IS  - 33
SP  - 6813
EP  - 6829
PB  - Royal Society of Chemistry
CY  - Cambridge
ER  - 
TY  - GEN
A1  - Kubin, Markus
A1  - Guo, Meiyuan
A1  - Kroll, Thomas
A1  - Löchel, Heike
A1  - Källman, Erik
A1  - Baker, Michael L.
A1  - Mitzner, Rolf
A1  - Gul, Sheraz
A1  - Kern, Jan
A1  - Föhlisch, Alexander
A1  - Erko, Alexei
A1  - Bergmann, Uwe
A1  - Yachandra, Vittal
A1  - Yano, Junko
A1  - Lundberg, Marcus
A1  - Wernet, Philippe
T1  - Probing the oxidation state of transition metal complexes
BT  - a case study on how charge and spin densities determine Mn L-edge X-ray absorption energies
T2  - Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe
N2  - Transition metals in inorganic systems and metalloproteins can occur in different oxidation states, which makes them ideal redox-active catalysts. To gain a mechanistic understanding of the catalytic reactions, knowledge of the oxidation state of the active metals, ideally in operando, is therefore critical. L-edge X-ray absorption spectroscopy (XAS) is a powerful technique that is frequently used to infer the oxidation state via a distinct blue shift of L-edge absorption energies with increasing oxidation state. A unified description accounting for quantum-chemical notions whereupon oxidation does not occur locally on the metal but on the whole molecule and the basic understanding that L-edge XAS probes the electronic structure locally at the metal has been missing to date. Here we quantify how charge and spin densities change at the metal and throughout the molecule for both redox and core-excitation processes. We explain the origin of the L-edge XAS shift between the high-spin complexes Mn-II(acac)(2) and Mn-III(acac)(3) as representative model systems and use ab initio theory to uncouple effects of oxidation-state changes from geometric effects. The shift reflects an increased electron affinity of Mn-III in the core-excited states compared to the ground state due to a contraction of the Mn 3d shell upon core-excitation with accompanied changes in the classical Coulomb interactions. This new picture quantifies how the metal-centered core hole probes changes in formal oxidation state and encloses and substantiates earlier explanations. The approach is broadly applicable to mechanistic studies of redox-catalytic reactions in molecular systems where charge and spin localization/delocalization determine reaction pathways.
T3  - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 656 
KW  - electronic-structure
KW  - atomic multiplet
KW  - water-oxidation
KW  - iron complexes
KW  - photosystem-II
KW  - spectroscopy
KW  - manganese
KW  - spectra
KW  - ligand
KW  - FE
Y1  - 2019
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-425057
SN  - 1866-8372
IS  - 656
ER  - 
TY  - JOUR
A1  - Kubin, Markus
A1  - Kern, Jan
A1  - Gul, Sheraz
A1  - Kroll, Thomas
A1  - Chatterjee, Ruchira
A1  - Loechel, Heike
A1  - Fuller, Franklin D.
A1  - Sierra, Raymond G.
A1  - Quevedo, Wilson
A1  - Weniger, Christian
A1  - Rehanek, Jens
A1  - Firsov, Anatoly
A1  - Laksmono, Hartawan
A1  - Weninger, Clemens
A1  - Alonso-Mori, Roberto
A1  - Nordlund, Dennis L.
A1  - Lassalle-Kaiser, Benedikt
A1  - Glownia, James M.
A1  - Krzywinski, Jacek
A1  - Moeller, Stefan
A1  - Turner, Joshua J.
A1  - Minitti, Michael P.
A1  - Dakovski, Georgi L.
A1  - Koroidov, Sergey
A1  - Kawde, Anurag
A1  - Kanady, Jacob S.
A1  - Tsui, Emily Y.
A1  - Suseno, Sandy
A1  - Han, Zhiji
A1  - Hill, Ethan
A1  - Taguchi, Taketo
A1  - Borovik, Andrew S.
A1  - Agapie, Theodor
A1  - Messinger, Johannes
A1  - Erko, Alexei
A1  - Föhlisch, Alexander
A1  - Bergmann, Uwe
A1  - Mitzner, Rolf
A1  - Yachandra, Vittal K.
A1  - Yano, Junko
A1  - Wernet, Philippe
T1  - Soft x-ray absorption spectroscopy of metalloproteins and high-valent metal-complexes at room temperature using free-electron lasers
JF  - Structural dynamics
N2  - X-ray absorption spectroscopy at the L-edge of 3d transition metals provides unique information on the local metal charge and spin states by directly probing 3d-derived molecular orbitals through 2p-3d transitions. However, this soft x-ray technique has been rarely used at synchrotron facilities for mechanistic studies of metalloenzymes due to the difficulties of x-ray-induced sample damage and strong background signals from light elements that can dominate the low metal signal. Here, we combine femtosecond soft x-ray pulses from a free-electron laser with a novel x-ray fluorescence-yield spectrometer to overcome these difficulties. We present L-edge absorption spectra of inorganic high-valent Mn complexes (Mn similar to 6-15 mmol/l) with no visible effects of radiation damage. We also present the first L-edge absorption spectra of the oxygen evolving complex (Mn4CaO5) in Photosystem II (Mn < 1 mmol/l) at room temperature, measured under similar conditions. Our approach opens new ways to study metalloenzymes under functional conditions. (C) 2017 Author(s).
Y1  - 2017
U6  - https://doi.org/10.1063/1.4986627
SN  - 2329-7778
VL  - 4
PB  - American Institute of Physics
CY  - Melville
ER  - 
TY  - JOUR
A1  - Kroll, Thomas
A1  - Kern, Jan
A1  - Kubin, Markus
A1  - Ratner, Daniel
A1  - Gul, Sheraz
A1  - Fuller, Franklin D.
A1  - Löchel, Heike
A1  - Krzywinski, Jacek
A1  - Lutman, Alberto
A1  - Ding, Yuantao
A1  - Dakovski, Georgi L.
A1  - Moeller, Stefan
A1  - Turner, Joshua J.
A1  - Alonso-Mori, Roberto
A1  - Nordlund, Dennis L.
A1  - Rehanek, Jens
A1  - Weniger, Christian
A1  - Firsov, Alexander
A1  - Brzhezinskaya, Maria
A1  - Chatterjee, Ruchira
A1  - Lassalle-Kaiser, Benedikt
A1  - Sierra, Raymond G.
A1  - Laksmono, Hartawan
A1  - Hill, Ethan
A1  - Borovik, Andrew S.
A1  - Erko, Alexei
A1  - Föhlisch, Alexander
A1  - Mitzner, Rolf
A1  - Yachandra, Vittal K.
A1  - Yano, Junko
A1  - Wernet, Philippe
A1  - Bergmann, Uwe
T1  - X-ray absorption spectroscopy using a self-seeded soft X-ray free-electron laser
JF  - Optics express : the international electronic journal of optics
N2  - X-ray free electron lasers (XFELs) enable unprecedented new ways to study the electronic structure and dynamics of transition metal systems. L-edge absorption spectroscopy is a powerful technique for such studies and the feasibility of this method at XFELs for solutions and solids has been demonstrated. However, the required x-ray bandwidth is an order of magnitude narrower than that of self-amplified spontaneous emission (SASE), and additional monochromatization is needed. Here we compare L-edge x-ray absorption spectroscopy (XAS) of a prototypical transition metal system based on monochromatizing the SASE radiation of the linac coherent light source (LCLS) with a new technique based on self-seeding of LCLS. We demonstrate how L-edge XAS can be performed using the self-seeding scheme without the need of an additional beam line monochromator. We show how the spectral shape and pulse energy depend on the undulator setup and how this affects the x-ray spectroscopy measurements. (C) 2016 Optical Society of America
Y1  - 2016
U6  - https://doi.org/10.1364/OE.24.022469
SN  - 1094-4087
VL  - 24
SP  - 22469
EP  - 22480
PB  - Optical Society of America
CY  - Washington
ER  - 
TY  - JOUR
A1  - Mitzner, Rolf
A1  - Rehanek, Jens
A1  - Kern, Jan
A1  - Gul, Sheraz
A1  - Hattne, Johan
A1  - Taguchi, Taketo
A1  - Alonso-Mori, Roberto
A1  - Tran, Rosalie
A1  - Weniger, Christian
A1  - Schröder, Henning
A1  - Quevedo, Wilson
A1  - Laksmono, Hartawan
A1  - Sierra, Raymond G.
A1  - Han, Guangye
A1  - Lassalle-Kaiser, Benedikt
A1  - Koroidov, Sergey
A1  - Kubicek, Katharina
A1  - Schreck, Simon
A1  - Kunnus, Kristjan
A1  - Brzhezinskaya, Maria
A1  - Firsov, Alexander
A1  - Minitti, Michael P.
A1  - Turner, Joshua J.
A1  - Möller, Stefan
A1  - Sauter, Nicholas K.
A1  - Bogan, Michael J.
A1  - Nordlund, Dennis
A1  - Schlotter, William F.
A1  - Messinger, Johannes
A1  - Borovik, Andrew S.
A1  - Techert, Simone
A1  - de Groot, Frank M. F.
A1  - Föhlisch, Alexander
A1  - Erko, Alexei
A1  - Bergmann, Uwe
A1  - Yachandra, Vittal K.
A1  - Wernet, Philippe
A1  - Yano, Junko
T1  - L-edge x-ray absorption spectroscopy of dilute systems relevant to metalloproteins using an X-ray free-electron laser
JF  - The journal of physical chemistry letters
N2  - L-edge spectroscopy of 3d transition metals provides important electronic structure information and has been used in many fields. However, the use of this method for studying dilute aqueous systems, such as metalloenzymes, has not been prevalent because of severe radiation damage and the lack of suitable detection systems. Here we present spectra from a dilute Mn aqueous solution using a high-transmission zone-plate spectrometer at the Linac Coherent Light Source (LCLS). The spectrometer has been optimized for discriminating the Mn L-edge signal from the overwhelming 0 K-edge background that arises from water and protein itself, and the ultrashort LCLS X-ray pulses can outrun X-ray induced damage. We show that the deviations of the partial-fluorescence yield-detected spectra from the true absorption can be well modeled using the state-dependence of the fluorescence yield, and discuss implications for the application of our concept to biological samples.
Y1  - 2013
U6  - https://doi.org/10.1021/jz401837f
SN  - 1948-7185
VL  - 4
IS  - 21
SP  - 3641
EP  - 3647
PB  - American Chemical Society
CY  - Washington
ER  - 
TY  - JOUR
A1  - Sellberg, Jonas A.
A1  - McQueen, Trevor A.
A1  - Laksmono, Hartawan
A1  - Schreck, Simon
A1  - Beye, Martin
A1  - DePonte, Daniel P.
A1  - Kennedy, Brian
A1  - Nordlund, Dennis
A1  - Sierra, Raymond G.
A1  - Schlesinger, Daniel
A1  - Tokushima, Takashi
A1  - Zhovtobriukh, Iurii
A1  - Eckert, Sebastian
A1  - Segtnan, Vegard H.
A1  - Ogasawara, Hirohito
A1  - Kubicek, Katharina
A1  - Techert, Simone
A1  - Bergmann, Uwe
A1  - Dakovski, Georgi L.
A1  - Schlotter, William F.
A1  - Harada, Yoshihisa
A1  - Bogan, Michael J.
A1  - Wernet, Philippe
A1  - Föhlisch, Alexander
A1  - Pettersson, Lars G. M.
A1  - Nilsson, Anders
T1  - X-ray emission spectroscopy of bulk liquid water in "no-man's land"
JF  - The journal of chemical physics : bridges a gap between journals of physics and journals of chemistr
N2  - The structure of bulk liquid water was recently probed by x-ray scattering below the temperature limit of homogeneous nucleation (T-H) of similar to 232 K [J. A. Sellberg et al., Nature 510, 381-384 (2014)]. Here, we utilize a similar approach to study the structure of bulk liquid water below T-H using oxygen K-edge x-ray emission spectroscopy (XES). Based on previous XES experiments [T. Tokushima et al., Chem. Phys. Lett. 460, 387-400 (2008)] at higher temperatures, we expected the ratio of the 1b(1)' and 1b(1)" peaks associated with the lone-pair orbital in water to change strongly upon deep supercooling as the coordination of the hydrogen (H-) bonds becomes tetrahedral. In contrast, we observed only minor changes in the lone-pair spectral region, challenging an interpretation in terms of two interconverting species. A number of alternative hypotheses to explain the results are put forward and discussed. Although the spectra can be explained by various contributions from these hypotheses, we here emphasize the interpretation that the line shape of each component changes dramatically when approaching lower temperatures, where, in particular, the peak assigned to the proposed disordered component would become more symmetrical as vibrational interference becomes more important. (C) 2015 AIP Publishing LLC.
Y1  - 2015
U6  - https://doi.org/10.1063/1.4905603
SN  - 0021-9606
SN  - 1089-7690
VL  - 142
IS  - 4
PB  - American Institute of Physics
CY  - Melville
ER  - 
TY  - JOUR
A1  - Schreck, Simon
A1  - Beye, Martin
A1  - Sellberg, Jonas A.
A1  - McQueen, Trevor
A1  - Laksmono, Hartawan
A1  - Kennedy, Brian
A1  - Eckert, Sebastian
A1  - Schlesinger, Daniel
A1  - Nordlund, Dennis
A1  - Ogasawara, Hirohito
A1  - Sierra, Raymond G.
A1  - Segtnan, Vegard H.
A1  - Kubicek, Katharina
A1  - Schlotter, William F.
A1  - Dakovski, Georgi L.
A1  - Moeller, Stefan P.
A1  - Bergmann, Uwe
A1  - Techert, Simone
A1  - Pettersson, Lars G. M.
A1  - Wernet, Philippe
A1  - Bogan, Michael J.
A1  - Harada, Yoshihisa
A1  - Nilsson, Anders
A1  - Föhlisch, Alexander
T1  - Reabsorption of soft x-ray emission at high x-ray free-electron laserfluences
JF  - Physical review letters
N2  - We report on oxygen K-edge soft x-ray emission spectroscopy from a liquid water jet at the Linac Coherent Light Source. We observe significant changes in the spectral content when tuning over a wide range of incident x-ray fluences. In addition the total emission yield decreases at high fluences. These modifications result from reabsorption of x-ray emission by valence-excited molecules generated by the Auger cascade. Our observations have major implications for future x-ray emission studies at intense x-ray sources. We highlight the importance of the x-ray pulse length with respect to the core-hole lifetime.
Y1  - 2014
U6  - https://doi.org/10.1103/PhysRevLett.113.153002
SN  - 0031-9007
SN  - 1079-7114
VL  - 113
IS  - 15
PB  - American Physical Society
CY  - College Park
ER  -