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Solution structure and excitation energy transfer in phycobiliproteins of Acaryochloris marina investigated by small angle scattering

M. Golub, S. Combet, DC. Wieland, D. Soloviov, A. Kuklin, H. Lokstein, FJ. Schmitt, R. Olliges, M. Hecht, HJ. Eckert, J. Pieper,

. 2017 ; 1858 (4) : 318-324. [pub] 20170126

Jazyk angličtina Země Nizozemsko

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc17031085

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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$a The structure of phycobiliproteins of the cyanobacterium Acaryochloris marina was investigated in buffer solution at physiological temperatures, i.e. under the same conditions applied in spectroscopic experiments, using small angle neutron scattering. The scattering data of intact phycobiliproteins in buffer solution containing phosphate can be well described using a cylindrical shape with a length of about 225Å and a diameter of approximately 100Å. This finding is qualitatively consistent with earlier electron microscopy studies reporting a rod-like shape of the phycobiliproteins with a length of about 250 (M. Chen et al., FEBS Letters 583, 2009, 2535) or 300Å (J. Marquart et al., FEBS Letters 410, 1997, 428). In contrast, phycobiliproteins dissolved in buffer lacking phosphate revealed a splitting of the rods into cylindrical subunits with a height of 28Å only, but also a pronounced sample aggregation. Complementary small angle neutron and X-ray scattering experiments on phycocyanin suggest that the cylindrical subunits may represent either trimeric phycocyanin or trimeric allophycocyanin. Our findings are in agreement with the assumption that a phycobiliprotein rod with a total height of about 225Å can accommodate seven trimeric phycocyanin subunits and one trimeric allophycocyanin subunit, each of which having a height of about 28Å. The structural information obtained by small angle neutron and X-ray scattering can be used to interpret variations in the low-energy region of the 4.5K absorption spectra of phycobiliproteins dissolved in buffer solutions containing and lacking phosphate, respectively.
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$a Combet, S $u Laboratoire Léon-Brillouin, CEA-CNRS, Université Paris-Saclay, CEA-Saclay, F-91191 Gif-sur-Yvette, France.
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$a Wieland, D C F $u Institute for Metalic Biomaterials, Helmholtz Zentrum Geesthacht, 21502 Geesthacht, Germany.
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$a Soloviov, D $u Joint Institute for Nuclear Research, Dubna, Russia; Moscow Institute of Physics and Technology, Dolgoprudny, Russia; Institute for Safety Problems of Nuclear Power Plants NAS of Ukraine, Kyiv, Ukraine.
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$a Kuklin, A $u Joint Institute for Nuclear Research, Dubna, Russia; Moscow Institute of Physics and Technology, Dolgoprudny, Russia.
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$a Lokstein, H $u Department of Chemical Physics and Optics, Charles University, Prague, Ke Karlovu 3, 121 16 Prague, Czech Republic.
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$a Schmitt, F-J $u Max-Volmer-Laboratories for Biophysical Chemistry, Technical University Berlin, Germany.
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$a Hecht, M $u Institute of Physics, University of Tartu, Tartu, Estonia.
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$a Eckert, H-J $u Max-Volmer-Laboratories for Biophysical Chemistry, Technical University Berlin, Germany.
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$a Pieper, J $u Institute of Physics, University of Tartu, Tartu, Estonia. Electronic address: pieper@ut.ee.
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