Photosynthesis Genes and LH1 Proteins of Roseospirillum Parvum 930I, a Purple Non-Sulfur Bacterium with Unusual Spectral Properties

Abstract

The purple bacterium Roseospirillum(Rss.)parvum 930I, like most other purple bacteria, contains bacteriochlorophyll (BChl)-a as a LH chromophore, but exhibits an extremely red-shifted Qy absorption maximum centered at 909 nm. The puf operon encoding the LH1 and other pigment-binding proteins was cloned and sequenced, revealing the gene structure pufBALMC. Comparative analysis of predicted amino acid sequences of the α- and β-core LH polypeptides (PufA and PufB) revealed five amino-acid substitutions at positions that are highly conserved in other purple bacteria. In the primary structure, these residues are in close proximity to the BChl-a ligating histidine residue (α+3, α+5, α+6 and β−4, β+9, with respect to the central histidine, His0). The nature of the enormous red-shifts to the near-infrared region of the light were attributed to those residues, with special emphasis to cysteine residues rarely present in other purple bacterial antenna polypeptides. Three-dimensional structural models of the Rss. parvum LH1-α and -β polypeptides suggest that the thiol groups of αCys+3 and βCys−4 are oriented toward the BChl-a macrocycle in the native antenna complex. Because of their predicted close proximity to BChl, these thiol groups are likely to modulate the spectral properties of the LH1 complex. Phylogenetic comparisons of LH1 polypeptides indicate that Rss. parvum-like amino-acid substitutions in proteobacterial LH1 complexes arose independently during evolution.