Spectrally pure B800-850 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 (alpha, beta) have been isolated by organic solvent extraction of the lyophilised B800-850 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. B800-850 alpha consists of 53 amino acids and is 45.3% and 50.9% homologous to the B800-850-alpha antenna polypeptides of Rhodobacter sphaeroides and Rhodobacter capsulatus, respectively. The second very short polypeptide (B800-850-beta, 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.

Amino Acid Sequence↗

PubMedDate not supplied

The primary structures of the core antenna polypeptides from Rhodopseudomonas marina.

The antenna complex B880 of Rp. marina has been isolated by applying ion-exchange chromatography on Whatman DE-52 resin and sucrose density centrifugation of LDAO-solubilized photosynthetic membranes. The antenna polypeptides B880-alpha and B880-beta were prepared by organic solvent extraction of extensively dialyzed and freeze-dried B880 antenna complex material or photosynthetic membranes. Gel filtration on Sephadex LH-60 and ion-exchange chromatography on Whatman DE-32 resin in the presence of organic solvents and an additional step on a C-8 reversed phase column yielded pure alpha- and beta-apoproteins. Their complete primary structures have been elucidated using automated Edman degradation and carboxypeptidase digestion. According to quantitative Edman degradation the ratio of B880-alpha and B880-beta has been determined as 1:1 in the isolated antenna complex as well as in the photosynthetic membrane. B880-alpha of Rp. marina, presumably N-formylated, consists of 52 amino acid residues and is 75, 56, 52 and 44% homologous to the corresponding core antenna polypeptides of Rs. rubrum, Rp. viridis, Rb. capsulatus and Rb. sphaeroides. In contrast, B880-beta (56 amino acid residues) is less homologous to the corresponding core beta-antenna polypeptides of the same strains (57, 51, 41 and 42%). It shows an extended N-terminal domain as compared to the B880-alpha polypeptide. Apart from the typical structural features of bacterial membrane-bound antenna polypeptides (three domain structure. His-residue in the hydrophobic stretch) the antenna polypeptides of Rp. marina are structurally related to polypeptides of core antenna complexes with strong near infrared circular dichroism signals.

Amino Acid Sequence↗

PubMedDate not supplied

The primary structure of the presumable BChl d-binding polypeptide of Chlorobium vibrioforme f. thiosulfatophilum.

In addition to the previous isolated and sequenced polypeptides from green photosynthetic sulfur bacteria, which are presumably involved in binding BChl c and e, an analogous polypeptide has been purified from the BChl d-containing bacterium Chlorobium vibrioforme f. thiosulfatophilum. The primary structure of this 6.15 kDa polypeptide was determined. It shows an extremely high homology (98.3%) to the corresponding polypeptide from Pelodictyon luteolum, indicative of an important functional role.

Amino Acid Sequence↗