Pigment conformation and pigment-protein interactions in the reconstituted Lhcb4 antenna protein.
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.
Pascal
A
A
Università di Verona, Facoltà di Scienze MM, FF, NN, Biotechnologie Vegetali, Italy. apascal@cea.fr
Gastaldelli
M
M
Ceoldo
S
S
Bassi
R
R
Robert
B
B
D002338:Carotenoids / Q000737:chemistry*; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics; D002734:Chlorophyll / Q000737:chemistry*; D000077194:Chlorophyll A; D016297:Mutagenesis, Site-Directed; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; D010940:Plant Proteins; D011994:Recombinant Proteins / Q000737:chemistry; D013059:Spectrum Analysis, Raman; D003313:Zea mays
D002352:Carrier Proteins; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; D010940:Plant Proteins; D011994:Recombinant Proteins; D002734:Chlorophyll; D002338:Carotenoids; C037184:chlorophyll b; D000077194:Chlorophyll A