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

• Published in: Biochimica et biophysica acta. Bioenergetics Vol. 1858; no. 4; pp. 318 - 324
• Main Authors: Golub, M., Combet, S., Wieland, D.C.F., Soloviov, D., Kuklin, A., Lokstein, H., Schmitt, F.-J., Olliges, R., Hecht, M., Eckert, H.-J., Pieper, J.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.04.2017
• Subjects: 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; 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
• ISSN: 0005-2728; 1879-2650
• DOI: 10.1016/j.bbabio.2017.01.010

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.