Selective Release, Removal, and Reconstitution of Bacteriochlorophyll a Molecules into the B800 Sites of LH2 Complexes from Rhodopseudomonas acidophila 10050

A method is described which allows the selective release and removal of the Bchla-B800 molecules from the LH2 complex of Rhodopseudomonas acidophila 10050. This procedure also allows reconstitution of ∼80% of the empty binding sites with native Bchla. As shown by circular dichroism spectroscopy, the...

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Bibliographic Details
Published in:Biochemistry (Easton) 1999-07, Vol.38 (30), p.9684-9692
Main Authors: Fraser, Niall J, Dominy, Peter J, Ücker, Beaté, Simonin, Ingrid, Scheer, Hugo, Cogdell, Richard J
Format: Article
Language:English
Subjects:
Bacterial Proteins
bacteriochlorophyll a
Bacteriochlorophylls - chemistry
Bacteriochlorophylls - metabolism
Binding Sites
Buffers
Circular Dichroism
Detergents
Energy Transfer
Glucosides
Intracellular Membranes - chemistry
Intracellular Membranes - metabolism
Light-Harvesting Protein Complexes
Photosynthetic Reaction Center Complex Proteins - chemistry
Photosynthetic Reaction Center Complex Proteins - isolation & purification
Photosynthetic Reaction Center Complex Proteins - metabolism
Photosystem II Protein Complex
Rhodopseudomonas - chemistry
Rhodopseudomonas - metabolism
Rhodopseudomonas acidophila
Temperature
Time Factors
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Summary:A method is described which allows the selective release and removal of the Bchla-B800 molecules from the LH2 complex of Rhodopseudomonas acidophila 10050. This procedure also allows reconstitution of ∼80% of the empty binding sites with native Bchla. As shown by circular dichroism spectroscopy, the overall structures of the B850-only and reconstituted complexes are not affected by the pigment-exchange procedure. The pigments reconstituted into the B800 sites can also efficiently transfer excitation energy to the Bchla-B850 molecules.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi990796i