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  • 1. Fuller, Franklin D
    et al.
    Gul, Sheraz
    Chatterjee, Ruchira
    Burgie, E Sethe
    Young, Iris D
    Lebrette, Hugo
    Srinivas, Vivek
    Brewster, Aaron S
    Michels-Clark, Tara
    Clinger, Jonathan A
    Andi, Babak
    Ibrahim, Mohamed
    Pastor, Ernest
    de Lichtenberg, Casper
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Hussein, Rana
    Pollock, Christopher J
    Zhang, Miao
    Stan, Claudiu A
    Kroll, Thomas
    Fransson, Thomas
    Weninger, Clemens
    Kubin, Markus
    Aller, Pierre
    Lassalle, Louise
    Brauer, Philipp
    Miller, Mitchell D
    Amin, Muhamed
    Koroidov, Sergey
    Umeå University, Faculty of Science and Technology, Department of Chemistry. Stanford PULSE Institute, SLAC National Accelerator Laboratory, Menlo Park, California, USA.
    Roessler, Christian G
    Allaire, Marc
    Sierra, Raymond G
    Docker, Peter T
    Glownia, James M
    Nelson, Silke
    Koglin, Jason E
    Zhu, Diling
    Chollet, Matthieu
    Song, Sanghoon
    Lemke, Henrik
    Liang, Mengning
    Sokaras, Dimosthenis
    Alonso-Mori, Roberto
    Zouni, Athina
    Messinger, Johannes
    Umeå University, Faculty of Science and Technology, Department of Chemistry. Department of Chemistry–Ångström, Molecular Biomimetics, Uppsala University, Uppsala, Sweden.
    Bergmann, Uwe
    Boal, Amie K
    Bollinger Jr, J Martin
    Krebs, Carsten
    Hogbom, Martin
    Phillips Jr, George N
    Vierstra, Richard D
    Sauter, Nicholas K
    Orville, Allen M
    Kern, Jan
    Yachandra, Vittal K
    Yano, Junko
    Drop-on-demand sample delivery for studying biocatalysts in action at X-ray free-electron lasers2017In: Nature Methods, ISSN 1548-7091, E-ISSN 1548-7105, Vol. 14, p. 443-449Article in journal (Refereed)
    Abstract [en]

    X-ray crystallography at X-ray free-electron laser sources is a powerful method for studying macromolecules at biologically relevant temperatures. Moreover, when combined with complementary techniques like X-ray emission spectroscopy, both global structures and chemical properties of metalloenzymes can be obtained concurrently, providing insights into the interplay between the protein structure and dynamics and the chemistry at an active site. The implementation of such a multimodal approach can be compromised by conflicting requirements to optimize each individual method. In particular, the method used for sample delivery greatly affects the data quality. We present here a robust way of delivering controlled sample amounts on demand using acoustic droplet ejection coupled with a conveyor belt drive that is optimized for crystallography and spectroscopy measurements of photochemical and chemical reactions over a wide range of time scales. Studies with photosystem II, the phytochrome photoreceptor, and ribonucleotide reductase R2 illustrate the power and versatility of this method.

  • 2. Kern, Jan
    et al.
    Alonso-Mori, Roberto
    Tran, Rosalie
    Hattne, Johan
    Gildea, Richard J.
    Echols, Nathaniel
    Glöckner, Carina
    Hellmich, Julia
    Laksmono, Hartawan
    Sierra, Raymond G.
    Lassalle-Kaiser, Benedikt
    Koroidov, Sergey
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Lampe, Alyssa
    Han, Guangye
    Gul, Sheraz
    Difiore, Dörte
    Milathianaki, Despina
    Fry, Alan R.
    Miahnahri, Alan
    Schafer, Donald W.
    Messerschmidt, Marc
    Seibert, M. Marvin
    Koglin, Jason E.
    Sokaras, Dimosthenis
    Weng, Tsu-Chien
    Sellberg, Jonas
    Latimer, Matthew J.
    Grosse-Kunstleve, Ralf W.
    Zwart, Petrus H.
    White, William E.
    Glatzel, Pieter
    Adams, Paul D.
    Bogan, Michael J.
    Williams, Garth J.
    Boutet, Sébastien
    Messinger, Johannes
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Zouni, Athina
    Sauter, Nicholas K.
    Yachandra, Vittal K.
    Bergmann, Uwe
    Yano, Junko
    Simultaneous Femtosecond X-ray Spectroscopy and Diffraction of Photosystem II at Room Temperature2013In: Science, ISSN 0036-8075, E-ISSN 1095-9203, Vol. 340, no 6131, p. 491-495Article in journal (Refereed)
    Abstract [en]

    Intense femtosecond x-ray pulses produced at the Linac Coherent Light Source (LCLS) were used for simultaneous x-ray diffraction (XRD) and x-ray emission spectroscopy (XES) of microcrystals of Photosystem II (PS II) at room temperature. This method probes the overall protein structure and the electronic structure of the Mn4CaO5 cluster in the oxygen-evolving complex of PS II. XRD data are presented from both the dark state (S1) and the first illuminated state (S2) of PS II. Our simultaneous XRD/XES study shows that the PS II crystals are intact during our measurements at the LCLS, not only with respect to the structure of PS II, but also with regard to the electronic structure of the highly radiation-sensitive Mn4CaO5 cluster, opening new directions for future dynamics studies.

  • 3. Kern, Jan
    et al.
    Tran, Rosalie
    Alonso-Mori, Roberto
    Koroidov, Sergey
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Echols, Nathaniel
    Hattne, Johan
    Ibrahim, Mohamed
    Gul, Sheraz
    Laksmono, Hartawan
    Sierra, Raymond G.
    Gildea, Richard J.
    Han, Guangye
    Hellmich, Julia
    Lassalle-Kaiser, Benedikt
    Chatterjee, Ruchira
    Brewster, Aaron S.
    Stan, Claudiu A.
    Gloeckner, Carina
    Lampe, Alyssa
    DiFiore, Doertee
    Milathianaki, Despina
    Fry, Alan R.
    Seibert, M. Marvin
    Koglin, Jason E.
    Gallo, Erik
    Uhlig, Jens
    Sokaras, Dimosthenis
    Weng, Tsu-Chien
    Zwart, Petrus H.
    Skinner, David E.
    Bogan, Michael J.
    Messerschmidt, Marc
    Glatzel, Pieter
    Williams, Garth J.
    Boutet, Sebastien
    Adams, Paul D.
    Zouni, Athina
    Messinger, Johannes
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Sauter, Nicholas K.
    Bergmann, Uwe
    Yano, Junko
    Yachandra, Vittal K.
    Taking snapshots of photosynthetic water oxidation using femtosecond X-ray diffraction and spectroscopy2014In: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 5, p. 4371-Article in journal (Refereed)
    Abstract [en]

    The dioxygen we breathe is formed by light-induced oxidation of water in photosystem II. O-2 formation takes place at a catalytic manganese cluster within milliseconds after the photosystem II reaction centre is excited by three single-turnover flashes. Here we present combined X-ray emission spectra and diffraction data of 2-flash (2F) and 3-flash (3F) photosystem II samples, and of a transient 3F' state (250 mu s after the third flash), collected under functional conditions using an X-ray free electron laser. The spectra show that the initial O-O bond formation, coupled to Mn reduction, does not yet occur within 250 mu s after the third flash. Diffraction data of all states studied exhibit an anomalous scattering signal from Mn but show no significant structural changes at the present resolution of 4.5 angstrom. This study represents the initial frames in a molecular movie of the structural changes during the catalytic reaction in photosystem II.

  • 4.
    Koroidov, Sergey
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Water splitting in natural and artificial photosynthetic systems2014Doctoral thesis, comprehensive summary (Other academic)
    Abstract [en]

    Photosynthesis is the unique biological process that converts carbon dioxide into organic compounds, for example sugars, using the energy of sunlight. Thereby solar energy is converted into chemical energy. Nearly all life depends on this reaction, either directly, or indirectly as the ultimate source of their food. Oxygenic photosynthesis occurs in plants, algae and cyanobacteria. This process created the present level of oxygen in the atmosphere, which allowed the formation of higher life, since respiration allows extracting up to 15-times more energy from organic matter than anaerobic fermentation. Oxygenic photosynthesis uses as substrate for the ubiquitous water. The light-induced oxidation of water to molecular oxygen (O2), catalyzed by the Mn4CaO5 cluster associated with the photosystem II (PS II) complex, is thus one of the most important and wide spread chemical processes occurring in the biosphere. Understanding the mechanism of water-oxidation by the Mn4CaO5 cluster is one of today’s great challenges in science. It is believed that one can extract basic principles of catalyst design from the natural system that than can be applied to artificial systems. Such systems can be used in the future for the generation of fuel from sunlight.

    In this thesis the light-induced production of molecular oxygen and carbon dioxide (CO2) by PSII was observed by membrane-inlet mass spectrometry. By analyzing this observation is shown that CO2 not only is the substrate in photosynthesis for the production of sugars, but that it also regulates the efficiency of the initial steps of the electron transport chain of oxygenic photosynthesis by acting, in form of HCO3-, as acceptor for protons produced during water-splitting. This finding concludes the 50-years old search for the function of CO2/HCO3 in photosynthetic water oxidation.

    For understanding the mechanism of water oxidation it is crucial to resolve the structures of all oxidation states, including transient once, of the Mn4CaO5 cluster. With this application in mind a new illumination setup was developed and characterized that allowed to bring the Mn4CaO5 cluster of PSII microcrystals into known oxidation states while they flow through a narrow capillary. The optimized illumination conditions were employed at the X-ray free electron laser at the Linac Coherent Light Source (LCLS) to obtain simultaneous x-ray diffraction (XRD) and x-ray emission spectroscopy (XES) at room temperature. This two methods probe the overall protein structure and the electronic structure of the Mn4CaO5 cluster, respectively. Data are presented from both the dark state (S1) and the first illuminated state (S2) of PS II. This approach opens new directions for studying structural changes during the catalytic cycle of the Mn4CaO5 cluster, and for resolving the mechanism of O-O bond formation.

    In two other projects the mechanism of molecular oxygen formation by artificial water oxidation catalysts containing inexpensive and abundant elements were studied. Oxygen evolution catalyzed by calcium manganese and manganese only oxides was studied in 18O-enriched water. It was concluded that molecular oxygen is formed by entirely different pathways depending on what chemical oxidant was used.  Only strong non-oxygen donating oxidants were found to support ‘true’ water-oxidation. For cobalt oxides a study was designed to understand the mechanistic details of how the O-O bond forms. The data demonstrate that O-O bond formation occurs by direct coupling between two terminal water-derived ligands. Moreover, by detailed theoretical modelling of the data the number of cobalt atoms per catalytic site was derived.

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  • 5.
    Koroidov, Sergey
    et al.
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Anderlund, Magnus F
    Styring, Stenbjörn
    Thapper, Anders
    Messinger, Johannes
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    First turnover analysis of water-oxidation catalyzed by Co-oxide nanoparticles2015In: Energy & Environmental Science, ISSN 1754-5692, E-ISSN 1754-5706, Vol. 8, no 8, p. 2492-2503Article in journal (Refereed)
    Abstract [en]

    Co-oxides are promising water oxidation catalysts for artificial photosynthesis devices. Presently, several different proposals exist for how they catalyze O-2 formation from water. Knowledge about this process at molecular detail will be required for their further improvement. Here we present time-resolved O-18-labelling isotope-ratio membrane-inlet mass spectrometry (MIMS) experiments to study the mechanism of water oxidation in Co/methylenediphosphonate (Co/M2P) oxide nanoparticles using [Ru(bpy)(3)](3+) (bpy = 2,2'-bipyridine) as chemical oxidant. We show that O-16-Co/M2P-oxide nanoparticles produce O-16(2) during their first turnover after simultaneous addition of (H2O)-O-18 and [Ru(bpy)(3)](3+), while sequential addition with a delay of 3 s yields oxygen reflecting bulk water O-18-enrichment. This result is interpreted to show that the O-O bond formation in Co/M2P-oxide nanoparticles occurs via intramolecular oxygen coupling between two terminal Co-OHn ligands that are readily exchangeable with bulk water in the resting state of the catalyst. Importantly, our data allow the determination of the number of catalytic sites within this amorphous nanoparticular material, to calculate the TOF per catalytic site and to derive the number of holes needed for the production of the first O-2 molecule per catalytic site. We propose that the mechanism of O-O bond formation during bulk catalysis in amorphous Co-oxides may differ from that taking place at the surface of crystalline materials.

  • 6.
    Koroidov, Sergey
    et al.
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Anderlund, Magnus F.
    Styring, Stenbjörn
    Thapper, Anders
    Messinger, Johannes
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Mechanism of water oxidation catalyzed by Co/M2P-oxides studied by isotope-ratio membrane inlet mass spectrometryManuscript (preprint) (Other academic)
    Abstract [en]

    Co-oxides are promising water oxidation catalysts for artificial photosynthesis devices. Their catalytic mechanism was studied previously both experimentally and theoretically, but there is presently no agreement whether the O-O bond formation occurs via nucleophilic attack or by direct coupling, and whether or not bridging oxygens participate as substrate during O-O bondformation. Here we present time-resolved 18O-labelling isotope-ratio membrane-inlet massspectrometry experiments employing the previously introduced Co/methylenediphosphonate (Co/M2P) system in combination with [Ru(bpy)3]3+ (bpy = 2,2’-bipyridine) as chemical oxidant. Our data demonstrate that for Co/M2P-oxide O-O bond formation occurs between two pre-bound, fast exchanging oxygen species, i.e. likely via direct coupling between two terminal water-derived oxygen ligands. Detailed modeling of the dependence of the O2-isotope ratios on the [Ru(bpy)3]3+ concentration revealed that in the Co/M2P-oxidenanoparticles almost all Co ions are catalytically active (2.35 Co per catalytic site) and that, starting from a ‘resting state‘, 3.5 electrons need to be removed from each catalytic site for thefirst O2 formation. Since it was previously demonstrated that in the resting state most Co ions are in the oxidation state Co(III), we conclude that the coupling mechanism involves at least one Co(IV)-O radical.

  • 7.
    Koroidov, Sergey
    et al.
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Shevela, Dmitriy
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Shutova, Tatyana
    Umeå University, Faculty of Science and Technology, Department of Plant Physiology. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).
    Samuelsson, Göran
    Umeå University, Faculty of Science and Technology, Department of Plant Physiology. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).
    Messinger, Johannes
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Mobile hydrogen carbonate acts as proton acceptor in photosynthetic water oxidation2014In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 11, no 17, p. 6299-6304Article in journal (Refereed)
    Abstract [en]

    Cyanobacteria, algae and plants oxidize water to the O2 we breathe, and consume CO2 during the synthesis of biomass. Although these vital processes are functionally and structurally well separated in photosynthetic organisms, there is a long-debated role for CO2/HCO3 in water oxidation. Using membrane-inlet mass spectrometry we demonstrate that HCO3 acts as a mobile proton acceptor that helps to transport the protons produced inside of photosystem II by water-oxidation out into the chloroplast's lumen, resulting in a light-driven production of O2 and CO2. Depletion of HCO3 from the media leads, in the absence of added buffers, to a reversible down-regulation of O2 production by about 20%. These findings add a previously unidentified component to the regulatory network of oxygenic photosynthesis, and conclude the more than 50-y-long quest for the function of CO2/ HCO3 in photosynthetic water oxidation.

  • 8. Kubin, Markus
    et al.
    Kern, Jan
    Gul, Sheraz
    Kroll, Thomas
    Chatterjee, Ruchira
    Löchel, Heike
    Fuller, Franklin D.
    Sierra, Raymond G.
    Quevedo, Wilson
    Weniger, Christian
    Rehanek, Jens
    Firsov, Anatoly
    Laksmono, Hartawan
    Weninger, Clemens
    Alonso-Mori, Roberto
    Nordlund, Dennis L.
    Lassalle-Kaiser, Benedikt
    Glownia, James M.
    Krzywinski, Jacek
    Moeller, Stefan
    Turner, Joshua J.
    Minitti, Michael P.
    Dakovski, Georgi L.
    Koroidov, Sergey
    Umeå University, Faculty of Science and Technology, Department of Chemistry. Stanford PULSE Institute, SLAC National Accelerator Laboratory, Menlo Park, California 94025, USA.
    Kawde, Anurag
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Kanady, Jacob S.
    Tsui, Emily Y.
    Suseno, Sandy
    Han, Zhiji
    Hill, Ethan
    Taguchi, Taketo
    Borovik, Andrew S.
    Agapie, Theodor
    Messinger, Johannes
    Umeå University, Faculty of Science and Technology, Department of Chemistry. Department of Chemistry, Molecular Biomimetics, Ångström Laboratory, Uppsala University, SE 75237 Uppsala, Sweden.
    Erko, Alexei
    Föhlisch, Alexander
    Bergmann, Uwe
    Mitzner, Rolf
    Yachandra, Vittal K.
    Yano, Junko
    Wernet, Philippe
    Soft x-ray absorption spectroscopy of metalloproteins and high-valent metal-complexes at room temperature using free-electron lasers2017In: Structural dynamics, ISSN 2329-7778, Vol. 4, no 5, article id 054307Article in journal (Refereed)
    Abstract [en]

    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.

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  • 9. Mitzner, Rolf
    et al.
    Rehanek, Jens
    Kern, Jan
    Gul, Sheraz
    Hattne, Johan
    Taguchi, Taketo
    Alonso-Mori, Roberto
    Tran, Rosalie
    Weniger, Christian
    Schroeder, Henning
    Quevedo, Wilson
    Laksmono, Hartawan
    Sierra, Raymond G.
    Han, Guangye
    Lassalle-Kaiser, Benedikt
    Koroidov, Sergey
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Kubicek, Katharina
    Schreck, Simon
    Kunnus, Kristjan
    Brzhezinskaya, Maria
    Firsov, Alexander
    Minitti, Michael P.
    Turner, Joshua J.
    Moeller, Stefan
    Sauter, Nicholas K.
    Bogan, Michael J.
    Nordlund, Dennis
    Schlotter, William F.
    Messinger, Johannes
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Borovik, Andrew
    Techert, Simone
    de Groot, Frank M. F.
    Foehlisch, Alexander
    Erko, Alexei
    Bergmann, Uwe
    Yachandra, Vittal K.
    Wernet, Philippe
    Yano, Junko
    L-Edge X-ray Absorption Spectroscopy of Dilute Systems Relevant to Metalloproteins Using an X-ray Free-Electron Laser2013In: Journal of Physical Chemistry Letters, ISSN 1948-7185, E-ISSN 1948-7185, Vol. 4, no 21, p. 3641-3647Article in journal (Refereed)
    Abstract [en]

    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.

  • 10. Sauter, Nicholas K.
    et al.
    Echols, Nathaniel
    Adams, Paul D.
    Zwart, Petrus H.
    Kern, Jan
    Brewster, Aaron S.
    Koroidov, Sergey
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Alonso-Mori, Roberto
    Zouni, Athina
    Messinger, Johannes
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Bergmann, Uwe
    Yano, Junko
    Yachandra, Vittal K.
    No observable conformational changes in PSII2016In: Nature, ISSN 0028-0836, E-ISSN 1476-4687, Vol. 533, no 7603, p. E1-E2Article in journal (Refereed)
  • 11.
    Shevela, Dmitriy
    et al.
    Umeå University, Faculty of Science and Technology, Department of Chemistry. Centre for Organelle Research, Faculty of Science and Technology, University of Stavanger, Stavanger, Norway.
    Arnold, Janine
    Reisinger, Veronika
    Berends, Hans-Martin
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Kmiec, Karol
    Koroidov, Sergey
    Umeå University, Faculty of Science and Technology, Department of Chemistry. PULSE Institute, SLAC National Accelerator Laboratory, Stanford University, Stanford, CA, USA.
    Bue, Ann Kristin
    Messinger, Johannes
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Eichacker, Lutz A.
    Biogenesis of water splitting by photosystem II during de-etiolation of barley (Hordeum vulgare L.)2016In: Plant, Cell and Environment, ISSN 0140-7791, E-ISSN 1365-3040, Vol. 39, no 7, p. 1524-1536Article in journal (Refereed)
    Abstract [en]

    Etioplasts lack thylakoid membranes and photosystem complexes. Light triggers differentiation of etioplasts into mature chloroplasts, and photosystem complexes assemble in parallel with thylakoid membrane development. Plastids isolated at various time points of de-etiolation are ideal to study the kinetic biogenesis of photosystem complexes during chloroplast development. Here, we investigated the chronology of photosystem II (PSII) biogenesis by monitoring assembly status of chlorophyll-binding protein complexes and development of water splitting via O2 production in plastids (etiochloroplasts) isolated during de-etiolation of barley (Hordeum vulgare L.). Assembly of PSII monomers, dimers and complexes binding outer light-harvesting antenna [PSII-light-harvesting complex II (LHCII) supercomplexes] was identified after 1, 2 and 4 h of de-etiolation, respectively. Water splitting was detected in parallel with assembly of PSII monomers, and its development correlated with an increase of bound Mn in the samples. After 4 h of de-etiolation, etiochloroplasts revealed the same water-splitting efficiency as mature chloroplasts. We conclude that the capability of PSII to split water during de-etiolation precedes assembly of the PSII-LHCII supercomplexes. Taken together, data show a rapid establishment of water-splitting activity during etioplast-to-chloroplast transition and emphasize that assembly of the functional water-splitting site of PSII is not the rate-limiting step in the formation of photoactive thylakoid membranes.

  • 12.
    Shevela, Dmitriy
    et al.
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Koroidov, Sergey
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Najafpour, M Mahdi
    Messinger, Johannes
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Kurz, Philipp
    Calcium manganese oxides as oxygen evolution catalysts: o(2) formation pathways indicated by (18) o-labelling studies2011In: Chemistry - A European Journal, ISSN 0947-6539, E-ISSN 1521-3765, Vol. 17, no 19, p. 5415-5423Article in journal (Refereed)
    Abstract [en]

    Oxygen evolution catalysed by calcium manganese and manganese-only oxides was studied in (18) O-enriched water. Using membrane-inlet mass spectrometry, we monitored the formation of the different O(2) isotopologues (16) O(2) , (16) O(18) O and (18) O(2) in such reactions simultaneously with good time resolution. From the analysis of the data, we conclude that entirely different pathways of dioxygen formation catalysis exist for reactions involving hydrogen peroxide (H(2) O(2) ), hydrogen persulfate (HSO(5) (-) ) or single-electron oxidants such as Ce(IV) and [Ru(III) (bipy)(3) ](3+) . Like the studied oxide catalysts, the active sites of manganese catalase and the oxygen-evolving complex (OEC) of photosystem II (PSII) consist of μ-oxido manganese or μ-oxido calcium manganese sites. The studied processes show very similar (18) O-labelling behaviour to the natural enzymes and are therefore interesting model systems for in vivo oxygen formation by manganese metalloenzymes such as PSII.

  • 13.
    Shevela, Dmitriy
    et al.
    Umeå University, Faculty of Science and Technology, Department of Chemistry. Max Planck Institute for Chemical Energy Conversion, Mülheim, Germany.
    Nöring, Birgit
    Max Planck Institute for Chemical Energy Conversion, Mülheim, Germany.
    Koroidov, Sergey
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Shutova, Tatyana
    Umeå University, Faculty of Science and Technology, Department of Plant Physiology. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).
    Samuelsson, Göran
    Umeå University, Faculty of Science and Technology, Department of Plant Physiology. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).
    Messinger, Johannes
    Umeå University, Faculty of Science and Technology, Department of Chemistry. Max Planck Institute for Chemical Energy Conversion, Mülheim, Germany.
    Efficiency of photosynthetic water oxidation at ambient and depleted levels of inorganic carbon2013In: Photosynthesis Research, ISSN 0166-8595, E-ISSN 1573-5079, Vol. 117, no 1-3, p. 401-412Article in journal (Refereed)
    Abstract [en]

    Over 40 years ago, Joliot et al. (Photochem Photobiol 10:309-329, 1969) designed and employed an elegant and highly sensitive electrochemical technique capable of measuring O2 evolved by photosystem II (PSII) in response to trains of single turn-over light flashes. The measurement and analysis of flash-induced oxygen evolution patterns (FIOPs) has since proven to be a powerful method for probing the turnover efficiency of PSII. Stemler et al. (Proc Natl Acad Sci USA 71(12):4679-4683, 1974), in Govindjee's lab, were the first to study the effect of "bicarbonate" on FIOPs by adding the competitive inhibitor acetate. Here, we extend this earlier work by performing FIOPs experiments at various, strictly controlled inorganic carbon (Ci) levels without addition of any inhibitors. For this, we placed a Joliot-type bare platinum electrode inside a N2-filled glove-box (containing 10-20 ppm CO2) and reduced the Ci concentration simply by washing the samples in Ci-depleted media. FIOPs of spinach thylakoids were recorded either at 20-times reduced levels of Ci or at ambient Ci conditions (390 ppm CO2). Numerical analysis of the FIOPs within an extended Kok model reveals that under Ci-depleted conditions the miss probability is discernibly larger (by 2-3 %) than at ambient conditions, and that the addition of 5 mM HCO3 (-) to the Ci-depleted thylakoids largely restores the original miss parameter. Since a "mild" Ci-depletion procedure was employed, we discuss our data with respect to a possible function of free or weakly bound HCO3 (-) at the water-splitting side of PSII.

  • 14. Tran, Rosalie
    et al.
    Kern, Jan
    Hattne, Johan
    Koroidov, Sergey
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Hellmich, Julia
    Alonso-Mori, Roberto
    Sauter, Nicholas K.
    Bergmann, Uwe
    Messinger, Johannes
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Zouni, Athina
    Yano, Junko
    Yachandra, Vittal K.
    The Mn4Ca photosynthetic water-oxidation catalyst studied by simultaneous X-ray spectroscopy and crystallography using an X-ray free-electron laser2014In: Philosophical Transactions of the Royal Society of London. Biological Sciences, ISSN 0962-8436, E-ISSN 1471-2970, Vol. 369, no 1647, p. 20130324-Article, review/survey (Refereed)
    Abstract [en]

    The structure of photosystem II and the catalytic intermediate states of the Mn4CaO5 cluster involved in water oxidation have been studied intensively over the past several years. An understanding of the sequential chemistry of light absorption and the mechanism of water oxidation, however, requires a new approach beyond the conventional steady-state crystallography and X-ray spectroscopy at cryogenic temperatures. In this report, we present the preliminary progress using an X-ray free-electron laser to determine simultaneously the light-induced protein dynamics via crystallography and the local chemistry that occurs at the catalytic centre using X-ray spectroscopy under functional conditions at room temperature.

  • 15. Young, Iris D.
    et al.
    Ibrahim, Mohamed
    Chatterjee, Ruchira
    Gul, Sheraz
    Fuller, Franklin D.
    Koroidov, Sergey
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Brewster, Aaron S.
    Tran, Rosalie
    Alonso-Mori, Roberto
    Kroll, Thomas
    Michels-Clark, Tara
    Laksmono, Hartawan
    Sierra, Raymond G.
    Stan, Claudiu A.
    Hussein, Rana
    Zhang, Miao
    Douthit, Lacey
    Kubin, Markus
    de Lichtenberg, Casper
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Vo Pham, Long
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Nilsson, Håkan
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Cheah, Mun Hon
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Shevela, Dmitriy
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Saracini, Claudio
    Bean, Mackenzie A.
    Seuffert, Ina
    Sokaras, Dimosthenis
    Weng, Tsu-Chien
    Pastor, Ernest
    Weninger, Clemens
    Fransson, Thomas
    Lassalle, Louise
    Bräuer, Philipp
    Aller, Pierre
    Docker, Peter T.
    Andi, Babak
    Orville, Allen M.
    Glownia, James M.
    Nelson, Silke
    Sikorski, Marcin
    Zhu, Diling
    Hunter, Mark S.
    Lane, Thomas J.
    Aquila, Andy
    Koglin, Jason E.
    Robinson, Joseph
    Liang, Mengning
    Boutet, Sébastien
    Lyubimov, Artem Y.
    Uervirojnangkoorn, Monarin
    Moriarty, Nigel W.
    Liebschner, Dorothee
    Afonine, Pavel V.
    Waterman, David G.
    Evans, Gwyndaf
    Wernet, Philippe
    Dobbek, Holger
    Weis, William I.
    Brunger, Axel T.
    Zwart, Petrus H.
    Adams, Paul D.
    Zouni, Athina
    Messinger, Johannes
    Umeå University, Faculty of Science and Technology, Department of Chemistry. Department of Chemistry, Molecular Biomimetics, Ångström Laboratory, Uppsala University.
    Bergmann, Uwe
    Sauter, Nicholas K.
    Kern, Jan
    Yachandra, Vittal K.
    Yano, Junko
    Structure of photosystem II and substrate binding at room temperature2016In: Nature, ISSN 0028-0836, E-ISSN 1476-4687, Vol. 540, no 7633, p. 453-457Article in journal (Refereed)
    Abstract [en]

    Light-induced oxidation of water by photosystem II (PS II) in plants, algae and cyanobacteria has generated most of the dioxygen in the atmosphere. PS II, a membrane-bound multi-subunit pigment protein complex, couples the one-electron photochemistry at the reaction centre with the four-electron redox chemistry of water oxidation at the Mn4CaO5 cluster in the oxygen-evolving complex (OEC). Under illumination, the OEC cycles through five intermediate S-states (S0 to S4)1, in which S1 is the dark-stable state and S3 is the last semi-stable state before O–O bond formation and O2 evolution2,3. A detailed understanding of the O–O bond formation mechanism remains a challenge, and will require elucidation of both the structures of the OEC in the different S-states and the binding of the two substrate waters to the catalytic site4–6. Here we report the use of femtosecond pulses from an X-ray free electron laser (XFEL) to obtain damage-free, room temperature structures of dark-adapted (S1), two-flash illuminated (2F; S3-enriched), and ammonia-bound two-flash illuminated (2F-NH3; S3-enriched) PS II. Although the recent 1.95 Å resolution structure of PS II at cryogenic temperature using an XFEL7 provided a damage-free view of the S1 state, measurements at room temperature are required to study the structural landscape of proteins under functional conditions8,9, and also for in situ advancement of the S-states. To investigate the water-binding site(s), ammonia, a water analogue, has been used as a marker, as it binds to the Mn4CaO5 cluster in the S2 and S3 states10. Since the ammonia-bound OEC is active, the ammonia-binding Mn site is not a substrate water site10–13. This approach, together with a comparison of the native dark and 2F states, is used to discriminate between proposed O–O bond formation mechanisms.

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