Spectrally pure B 800-850 light harvesting complexes of Rhodopseudomonas acidophila 7750 were prepared by chromatography of LDAO-solubilised photosynthetic membranes on Whatmann DE-52 ion exchange resin. Two low molecular mass polypeptides (α, β) have been isolated by organic solvent extraction of the lyophilised B 800-850 light harvesting complexes. Their primary structures were determined by liquid phase sequencer runs, by the sequence analyses of C-terminal o-iodosobenzoic acid fragments, by hydrazinolysis and by carboxypeptidase degradation. B 800-850-a consists of 53 amino acids and is 45.3% and 50.9% homologous to the B 800-850- a antenna polypeptides of Rhodobacter sphaeroides and Rhodobacter capsulatus, respectively. The second very short polypeptide (B800-850-β, 41 amino acids) is 61.0% and 56.1% homologous to the corresponding polypeptides of Rb. sphaeroides and Rb. capsulatus. The molar ratio of the two polypeptides is about 1:1. Both polypeptides show a hydrophilic N-terminal domain, a very hydrophobic central domain and a short C-terminal domain. In both polypeptides the typical His residues, identified in all antenna polypeptides of purple nonsulphur bacteria as possible bacteriochlorophyll binding sites, were found

Antenna polypeptides from two species of the family Ectothiorhodospiraceae have been investigated. By means of gel filtration and subsequent high‐performance liquid chromatography, at least five polypeptides were isolated from each of Ectothiorhodospira halochloris and Ectothiorhodospira halophila. The majority of their primary structures was identified by Edman degradation. Comparison of these polypeptide sequences with the known primary structures of antenna polypeptides from various purple non‐sulfur bacteria revealed interesting new aspects with regard to the structure of the core‐peripheral antenna system. E. halochloris and E. halophila contain two pairs of α‐ and β‐polypeptides each with typical primary structure elements of core complexes, indicating a modified antenna complex organization.

Whole cells from Ectothiorhodospira halochloris were extracted with an organic solvent mixture. At least five small hydrophobic polypeptides representing most probably the light harvesting polypeptides were purified by gel filtration and consecutive FPLC-RP chromatography. The complete amino acid sequence of a 7.4 kDa polypeptide was determined. The polypeptide shows a three domain structure, indicative of an integral membrane protein, similar to the structure of the light-harvesting polypeptides from purple non-sulfur bacteria. Sequence homologies to the fl-LHPs of purple bacteria range from 23. !% to 36.4~;. The conserved intramembrane located histidine residue of the antenna polypeptides of purple non-sulfur bacteria, assigned as the possible binding site for bacteriochlorophyll, was found to be replaced by asparagine.Purple bacteria; Bacteriochlorophyll b; Light-harvesting polypeptide; Amino acid sequence; (Ectothiorhodospira halochloris)

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