Pigment conformation and pigment–protein interactions in the reconstituted Lhcb4 antenna protein

FEBS Letters

Gastaldelli, Mirko¹  Ceoldo, Stefania¹  Pascal, Andy¹  Robert, Bruno²  Bassi, Roberto¹ 

[1] Università di Verona, Facoltà di Scienze MM.FF.NN., Biotechnologie Vegetali, Strada Le Grazie, 37134 Verona, Italy;Section de Biophysique des Protéines et des Membranes, DBCM/CEA&URA 2096/CNRS, CE-Saclay, 91191 Gif-sur-Yvette Cedex, France

关键词: Light-harvesting protein;    LHC gene family;    Chlorophyll binding;    Pigment–protein interaction;    Photosystem II;    Resonance Raman spectroscopy;    chl;    chlorophyll;    DDM;    β-dodecyl maltoside;    LHC;    light-harvesting complex;   

DOI  :  10.1016/S0014-5793(01)02228-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Resonance Raman spectra of the native Lhcb4 antenna protein are compared with those of a recombinant protein prepared by in vitro refolding of its polypeptide, over-expressed in Escherichia coli, with added pigments [Giuffra et al. (1996) Eur. J. Biochem. 238, 112–120]. The results indicate that the native pigment conformation is reproduced almost perfectly in the reconstituted protein, with only small differences which are attributed to a slight shift in the Soret absorption peak of two or more chlorophylls. This procedure therefore represents a model system for the investigation of site-directed mutant LHC proteins, which are otherwise very difficult to obtain.

【 授权许可】

Unknown