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

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11320%2F17%3A10367380" target="_blank" >RIV/00216208:11320/17:10367380 - isvavai.cz</a>

Result on the web

<a href="http://dx.doi.org/10.1016/j.bbabio.2017.01.010" target="_blank" >http://dx.doi.org/10.1016/j.bbabio.2017.01.010</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.bbabio.2017.01.010" target="_blank" >10.1016/j.bbabio.2017.01.010</a>

Result language

angličtina

Original language name

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

Original language description

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 225 angstrom and a diameter of approximately 100 A. 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 300 angstrom (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 28 A 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 225 A can accommodate seven trimeric phycocyanin subunits and one trimeric allophycocyanin subunit, each of which having a height of about 28 A. 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 4.5 K absorption spectra of phycobiliproteins dissolved in buffer solutions containing and lacking phosphate, respectively.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10610 - Biophysics

Project

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Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2017

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Biochimica et Biophysica Acta - Bioenergetics

ISSN

0005-2728

e-ISSN

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Volume of the periodical

1858

Issue of the periodical within the volume

4

Country of publishing house

NL - THE KINGDOM OF THE NETHERLANDS

Number of pages

7

Pages from-to

318-324

UT code for WoS article

000397369900006

EID of the result in the Scopus database

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