Abstract:
:Green sulfur bacteria possess two light-harvesting antenna systems, the chlorosome and the Fenna-Matthews-Olson (FMO) protein. In addition to self-aggregated bacteriochlorophyll (BChl) c, chlorosomes of Chlorobium tepidum contain a small amount of BChl a (ratio 100:1). The chlorosomal BChl a is associated with CsmA, a 6.2 kDa protein that accounts for more than 50% of the protein content of chlorosomes. This CsmA-BChl a complex is located in the chlorosome baseplate with the hydrophilic C-terminal part of CsmA in contact with the FMO protein. CsmA was purified from Chl. tepidum. Isolated chlorosomes were lyophilized and extracted with chloroform/methanol (1:1, v/v). The extract was further purified using gel filtration and reverse-phase HPLC and the purity of the preparation confirmed by SDS-PAGE. Mass spectrometric analysis showed an m/z of 6154.8, in agreement with the calculated mass of the csmA gene product after C-terminal processing. CD spectroscopy of the isolated protein showed that the main structural motif was an alpha-helix. We have reconstituted the isolated CsmA protein with BChl a in micelles of n-octyl beta-d-glucopyranoside. The resulting preparation reproduced the spectral characteristics of the CsmA-BChl a complex present in the chlorosome baseplate.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Pedersen MØ,Pham L,Steensgaard DB,Miller Mdoi
10.1021/bi701616rsubject
Has Abstractpub_date
2008-02-05 00:00:00pages
1435-41issue
5eissn
0006-2960issn
1520-4995journal_volume
47pub_type
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