L-Edge X-ray Absorption Spectroscopy of Dilute Systems Relevant to Metalloproteins Using an X-ray Free-Electron Laser.

PubWeight™: 0.89‹?›

🔗 View Article (PMID 24466387)

Published in J Phys Chem Lett on October 09, 2013

Authors

Rolf Mitzner1, Jens Rehanek2, Jan Kern3, Sheraz Gul4, Johan Hattne4, Taketo Taguchi5, Roberto Alonso-Mori6, Rosalie Tran4, Christian Weniger1, Henning Schröder7, Wilson Quevedo1, Hartawan Laksmono8, Raymond G Sierra8, Guangye Han4, Benedikt Lassalle-Kaiser4, Sergey Koroidov9, Katharina Kubicek10, Simon Schreck7, Kristjan Kunnus7, Maria Brzhezinskaya2, Alexander Firsov2, Michael P Minitti6, Joshua J Turner6, Stefan Moeller6, Nicholas K Sauter4, Michael J Bogan8, Dennis Nordlund11, William F Schlotter6, Johannes Messinger9, Andrew Borovik5, Simone Techert12, Frank M F de Groot13, Alexander Föhlisch7, Alexei Erko2, Uwe Bergmann6, Vittal K Yachandra4, Philippe Wernet1, Junko Yano4

Author Affiliations

1: Institute for Methods and Instrumentation for Synchrotron Radiation Research, Helmholtz-Zentrum Berlin für Materialien und Energie GmbH, 12489 Berlin, Germany.
2: Institute for Nanometre Optics and Technology, Helmholtz-Zentrum Berlin für Materialien und Energie GmbH, 12489 Berlin, Germany.
3: Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, United States ; LCLS, SLAC National Accelerator Laboratory, Menlo Park, California 94025, United States.
4: Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, United States.
5: Department of Chemistry, University of California-Irvine, 1102 Natural Sciences II, Irvine, California 92697, United States.
6: LCLS, SLAC National Accelerator Laboratory, Menlo Park, California 94025, United States.
7: Institute for Methods and Instrumentation for Synchrotron Radiation Research, Helmholtz-Zentrum Berlin für Materialien und Energie GmbH, 12489 Berlin, Germany ; Institut für Physik und Astronomie, Universität Potsdam, 14476 Potsdam, Germany.
8: Stanford PULSE Institute, SLAC National Accelerator Laboratory, Menlo Park, California 94025, United States.
9: Institutionen för Kemi, Kemiskt Biologiskt Centrum, Umeå Universitet, 901 87 Umeå, Sweden.
10: Stanford PULSE Institute, SLAC National Accelerator Laboratory, Menlo Park, California 94025, United States ; Structural Dynamics of (Bio)Chemical Systems, Deutsches Elektronen-Synchtrotron (DESY), Notkestrasse 85, 22607 Hamburg, Germany.
11: SSRL, SLAC National Accelerator Laboratory, Menlo Park, California 94025, United States.
12: Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany ; Structural Dynamics of (Bio)Chemical Systems, Deutsches Elektronen-Synchtrotron (DESY), Notkestrasse 85, 22607 Hamburg, Germany.
13: Inorganic Chemistry and Catalysis, Utrecht University, 3584 CG Utrecht, The Netherlands.

Articles cited by this

Femtosecond X-ray protein nanocrystallography. Nature (2011) 14.34

High-resolution protein structure determination by serial femtosecond crystallography. Science (2012) 6.90

X-ray damage to the Mn4Ca complex in single crystals of photosystem II: a case study for metalloprotein crystallography. Proc Natl Acad Sci U S A (2005) 4.05

Simultaneous femtosecond X-ray spectroscopy and diffraction of photosystem II at room temperature. Science (2013) 3.60

Room temperature femtosecond X-ray diffraction of photosystem II microcrystals. Proc Natl Acad Sci U S A (2012) 2.43

Nanoflow electrospinning serial femtosecond crystallography. Acta Crystallogr D Biol Crystallogr (2012) 2.32

Linac Coherent Light Source soft x-ray materials science instrument optical design and monochromator commissioning. Rev Sci Instrum (2011) 1.53

Where water is oxidized to dioxygen: structure of the photosynthetic Mn4Ca cluster from X-ray spectroscopy. Inorg Chem (2008) 1.47

The soft x-ray instrument for materials studies at the linac coherent light source x-ray free-electron laser. Rev Sci Instrum (2012) 1.36

Energy-dispersive X-ray emission spectroscopy using an X-ray free-electron laser in a shot-by-shot mode. Proc Natl Acad Sci U S A (2012) 1.33

The manganese(IV)/iron(III) cofactor of Chlamydia trachomatis ribonucleotide reductase: structure, assembly, radical initiation, and evolution. Curr Opin Struct Biol (2008) 1.11

A setup for resonant inelastic soft x-ray scattering on liquids at free electron laser light sources. Rev Sci Instrum (2012) 1.11

Fe L- and K-edge XAS of low-spin ferric corrole: bonding and reactivity relative to low-spin ferric porphyrin. Inorg Chem (2009) 1.06

Determination of absorption coefficients for concentrated samples by fluorescence detection. Phys Rev B Condens Matter (1993) 1.05

Probing the electronic structure of the hemoglobin active center in physiological solutions. Phys Rev Lett (2009) 1.04

Iron L-edge X-ray absorption spectroscopy of oxy-picket fence porphyrin: experimental insight into Fe-O2 bonding. J Am Chem Soc (2013) 1.03

Fe L-edge X-ray absorption spectroscopy of low-spin heme relative to non-heme Fe complexes: delocalization of Fe d-electrons into the porphyrin ligand. J Am Chem Soc (2007) 1.03

Ab Initio Calculations of X-ray Spectra: Atomic Multiplet and Molecular Orbital Effects in a Multiconfigurational SCF Approach to the L-Edge Spectra of Transition Metal Complexes. J Phys Chem Lett (2012) 0.98

A combined DFT and restricted open-shell configuration interaction method including spin-orbit coupling: application to transition metal L-edge X-ray absorption spectroscopy. J Chem Phys (2013) 0.98

On the enzymatic activity of catalase: an iron L-edge X-ray absorption study of the active centre. Phys Chem Chem Phys (2010) 0.94

Non-heme manganese catalase--the 'other' catalase. Arch Biochem Biophys (2011) 0.93

A sample holder for soft x-ray absorption spectroscopy of liquids in transmission mode. Rev Sci Instrum (2011) 0.93

Investigation of protein conformation and interactions with salts via X-ray absorption spectroscopy. Proc Natl Acad Sci U S A (2010) 0.88

Intrinsic deviations in fluorescence yield detected x-ray absorption spectroscopy: the case of the transition metal L₂,₃ edges. J Phys Condens Matter (2012) 0.87

Direct observation of molecular orbital mixing in a solvated organometallic complex. Angew Chem Int Ed Engl (2013) 0.87

Probing the hydrogen-bond network of water via time-resolved soft X-ray spectroscopy. Phys Chem Chem Phys (2009) 0.83

Dark channel fluorescence observations result from concentration effects rather than solvent-solute charge transfer. Nat Chem (2012) 0.80

Dips and peaks in fluorescence yield X-ray absorption are due to state-dependent decay. Nat Chem (2012) 0.79

High-valent [MnFe] and [FeFe] cofactors in ribonucleotide reductases. Biochim Biophys Acta (2011) 0.79

Electronic structure of ions and molecules in solution: a view from modern soft X-ray spectroscopies. Chem Soc Rev (2013) 0.79

Dissecting Local Atomic and Intermolecular Interactions of Transition-Metal Ions in Solution with Selective X-ray Spectroscopy. J Phys Chem Lett (2012) 0.78

Ligand discrimination of myoglobin in solution: an iron L-edge X-ray absorption study of the active centre. Chem Commun (Camb) (2013) 0.77