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  Purification, crystallization, NMR spectroscopy and biochemical analyses of alpha-phycoerythrocyanin peptides

Wiegand, G., Parbel, A., Seifert, M. H. J., Holak, T. A., & Reuter, W. (2002). Purification, crystallization, NMR spectroscopy and biochemical analyses of alpha-phycoerythrocyanin peptides. European Journal of Biochemistry, 269(20), 5046-5055.

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Genre: Journal Article
Alternative Title : Eur. J. Biochem.

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 Creators:
Wiegand, G.1, Author              
Parbel, A., Author
Seifert, M. H. J.2, Author              
Holak, T. A.2, Author              
Reuter, W.1, Author              
Affiliations:
1Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              
2Holak, Tad / NMR Spectroscopy, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565154              

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Free keywords: phycobilisomes; phycoerythrocyanin; protein structure; photochemistry; energy transfer
 Abstract: The alpha-phycoerythrocyanin subunits of the different phycoerythrocyanin complexes of the phycobilisomes from the cyanobacterium Mastigocladus laminosus perform a remarkable photochemistry. Similar to phytochromes - the photoreceptors of higher plants - the spectral properties of the molecule reversibly change according to the irradiation wavelength. To enable extensive analyses, the protein has been produced at high yield by improving purification protocols. As a result, several comparative studies on the Z - and E -configurations of the intact alpha-subunit, and also on photoactive peptides originating from nonspecific degradations of the chromoprotein, were possible. The analyses comprise absorbance, fluorescence and CD spectroscopy, crystallization, preliminary X-ray measurements, mass spectrometry, N-terminal amino acid sequencing and 1D NMR spectroscopy. Intact alpha- phycoerythrocyanin aggregates significantly, due to hydrophobic interactions between the two N-terminal helices. Removal of these helices reduces the aggregation but also destabilizes the protein fold. The complete subunit could be crystallized in its E -configuration, but the X-ray measurement conditions must be improved. Nevertheless, NMR spectroscopy on a soluble photoactive peptide presents the first insight into the complex chromophore protein interactions that are dependent on the light induced state. The chromophore environment in the Z - configuration is rigid whereas other regions of the protein are more flexible. In contrast, the E -configuration has a mobile chromophore, especially the pyrrole ring D, while other regions of the protein rigidified compared to the Z -configuration.

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Language(s): eng - English
 Dates: 2002-10
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 39197
ISI: 000178608400016
 Degree: -

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Title: European Journal of Biochemistry
  Alternative Title : Eur. J. Biochem.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 269 (20) Sequence Number: - Start / End Page: 5046 - 5055 Identifier: ISSN: 0014-2956