Solution structure and excitation energy transfer in phycobiliproteins of Acaryochloris marina investigated by small angle scattering
The structure of phycobiliproteins of the cyanobacterium Acaryochloris marina was investigated in buffer solution at physiological temperatures, i.e. under the same conditions applied in spectroscopic experiments, using small angle neutron scattering. The scattering data of intact phycobiliproteins...
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Published in | Biochimica et biophysica acta. Bioenergetics Vol. 1858; no. 4; pp. 318 - 324 |
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Main Authors | , , , , , , , , , , |
Format | Journal Article |
Language | English |
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Elsevier B.V
01.04.2017
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Abstract | The structure of phycobiliproteins of the cyanobacterium Acaryochloris marina was investigated in buffer solution at physiological temperatures, i.e. under the same conditions applied in spectroscopic experiments, using small angle neutron scattering. The scattering data of intact phycobiliproteins in buffer solution containing phosphate can be well described using a cylindrical shape with a length of about 225Å and a diameter of approximately 100Å. This finding is qualitatively consistent with earlier electron microscopy studies reporting a rod-like shape of the phycobiliproteins with a length of about 250 (M. Chen et al., FEBS Letters 583, 2009, 2535) or 300Å (J. Marquart et al., FEBS Letters 410, 1997, 428). In contrast, phycobiliproteins dissolved in buffer lacking phosphate revealed a splitting of the rods into cylindrical subunits with a height of 28Å only, but also a pronounced sample aggregation. Complementary small angle neutron and X-ray scattering experiments on phycocyanin suggest that the cylindrical subunits may represent either trimeric phycocyanin or trimeric allophycocyanin. Our findings are in agreement with the assumption that a phycobiliprotein rod with a total height of about 225Å can accommodate seven trimeric phycocyanin subunits and one trimeric allophycocyanin subunit, each of which having a height of about 28Å. The structural information obtained by small angle neutron and X-ray scattering can be used to interpret variations in the low-energy region of the 4.5K absorption spectra of phycobiliproteins dissolved in buffer solutions containing and lacking phosphate, respectively.
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•Small angle scattering reveals the solution structure of phycobiliproteins of Acaryochloris marina.•Intact phycobiliproteins in buffer containing phosphate exhibit a rod-shaped structure.•Phycobiliproteins in buffer lacking phosphate revealed a splitting into trimeric subunits. |
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AbstractList | The structure of phycobiliproteins of the cyanobacterium Acaryochloris marina was investigated in buffer solution at physiological temperatures, i.e. under the same conditions applied in spectroscopic experiments, using small angle neutron scattering. The scattering data of intact phycobiliproteins in buffer solution containing phosphate can be well described using a cylindrical shape with a length of about 225Å and a diameter of approximately 100Å. This finding is qualitatively consistent with earlier electron microscopy studies reporting a rod-like shape of the phycobiliproteins with a length of about 250 (M. Chen et al., FEBS Letters 583, 2009, 2535) or 300Å (J. Marquart et al., FEBS Letters 410, 1997, 428). In contrast, phycobiliproteins dissolved in buffer lacking phosphate revealed a splitting of the rods into cylindrical subunits with a height of 28Å only, but also a pronounced sample aggregation. Complementary small angle neutron and X-ray scattering experiments on phycocyanin suggest that the cylindrical subunits may represent either trimeric phycocyanin or trimeric allophycocyanin. Our findings are in agreement with the assumption that a phycobiliprotein rod with a total height of about 225Å can accommodate seven trimeric phycocyanin subunits and one trimeric allophycocyanin subunit, each of which having a height of about 28Å. The structural information obtained by small angle neutron and X-ray scattering can be used to interpret variations in the low-energy region of the 4.5K absorption spectra of phycobiliproteins dissolved in buffer solutions containing and lacking phosphate, respectively. The structure of phycobiliproteins of the cyanobacterium Acaryochloris marina was investigated in buffer solution at physiological temperatures, i.e. under the same conditions applied in spectroscopic experiments, using small angle neutron scattering. The scattering data of intact phycobiliproteins in buffer solution containing phosphate can be well described using a cylindrical shape with a length of about 225Å and a diameter of approximately 100Å. This finding is qualitatively consistent with earlier electron microscopy studies reporting a rod-like shape of the phycobiliproteins with a length of about 250 (M. Chen et al., FEBS Letters 583, 2009, 2535) or 300Å (J. Marquart et al., FEBS Letters 410, 1997, 428). In contrast, phycobiliproteins dissolved in buffer lacking phosphate revealed a splitting of the rods into cylindrical subunits with a height of 28Å only, but also a pronounced sample aggregation. Complementary small angle neutron and X-ray scattering experiments on phycocyanin suggest that the cylindrical subunits may represent either trimeric phycocyanin or trimeric allophycocyanin. Our findings are in agreement with the assumption that a phycobiliprotein rod with a total height of about 225Å can accommodate seven trimeric phycocyanin subunits and one trimeric allophycocyanin subunit, each of which having a height of about 28Å. The structural information obtained by small angle neutron and X-ray scattering can be used to interpret variations in the low-energy region of the 4.5K absorption spectra of phycobiliproteins dissolved in buffer solutions containing and lacking phosphate, respectively. [Display omitted] •Small angle scattering reveals the solution structure of phycobiliproteins of Acaryochloris marina.•Intact phycobiliproteins in buffer containing phosphate exhibit a rod-shaped structure.•Phycobiliproteins in buffer lacking phosphate revealed a splitting into trimeric subunits. |
Author | Pieper, J. Eckert, H.-J. Wieland, D.C.F. Olliges, R. Combet, S. Soloviov, D. Schmitt, F.-J. Golub, M. Kuklin, A. Lokstein, H. Hecht, M. |
Author_xml | – sequence: 1 givenname: M. surname: Golub fullname: Golub, M. organization: Institute of Physics, University of Tartu, Tartu, Estonia – sequence: 2 givenname: S. surname: Combet fullname: Combet, S. organization: Laboratoire Léon-Brillouin, CEA-CNRS, Université Paris-Saclay, CEA-Saclay, F-91191 Gif-sur-Yvette, France – sequence: 3 givenname: D.C.F. surname: Wieland fullname: Wieland, D.C.F. organization: Institute for Metalic Biomaterials, Helmholtz Zentrum Geesthacht, 21502 Geesthacht, Germany – sequence: 4 givenname: D. orcidid: 0000-0001-7945-2218 surname: Soloviov fullname: Soloviov, D. organization: Joint Institute for Nuclear Research, Dubna, Russia – sequence: 5 givenname: A. surname: Kuklin fullname: Kuklin, A. organization: Joint Institute for Nuclear Research, Dubna, Russia – sequence: 6 givenname: H. orcidid: 0000-0001-6739-4612 surname: Lokstein fullname: Lokstein, H. organization: Department of Chemical Physics and Optics, Charles University, Prague, Ke Karlovu 3, 121 16 Prague, Czech Republic – sequence: 7 givenname: F.-J. surname: Schmitt fullname: Schmitt, F.-J. organization: Max-Volmer-Laboratories for Biophysical Chemistry, Technical University Berlin, Germany – sequence: 8 givenname: R. surname: Olliges fullname: Olliges, R. organization: Max-Volmer-Laboratories for Biophysical Chemistry, Technical University Berlin, Germany – sequence: 9 givenname: M. surname: Hecht fullname: Hecht, M. organization: Institute of Physics, University of Tartu, Tartu, Estonia – sequence: 10 givenname: H.-J. orcidid: 0000-0002-0475-282X surname: Eckert fullname: Eckert, H.-J. organization: Max-Volmer-Laboratories for Biophysical Chemistry, Technical University Berlin, Germany – sequence: 11 givenname: J. surname: Pieper fullname: Pieper, J. email: pieper@ut.ee organization: Institute of Physics, University of Tartu, Tartu, Estonia |
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Keywords | Phycobiliproteins Acaryochloris marina Chl Excitation energy transfer SLD PBP +P PCB SAXS PS II PBP –P PC APC Small angle neutron scattering EET SANS A. marina T. elongatus Small angle X-ray scattering PBP |
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SubjectTerms | Acaryochloris marina Cyanobacteria - chemistry Energy Transfer Excitation energy transfer Neutron Diffraction Phycobiliproteins Phycobiliproteins - chemistry Scattering, Small Angle Small angle neutron scattering Small angle X-ray scattering X-Ray Diffraction |
Title | Solution structure and excitation energy transfer in phycobiliproteins of Acaryochloris marina investigated by small angle scattering |
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