Single core polypeptide in the reaction center of the photosynthetic bacterium Heliobacillus mobilis : structural implications and relations to other photosystems

摘要: Abstract The gene for a reaction center core polypeptide from the anoxygenic photosynthetic bacterium Heliobacillus mobilis was cloned and sequenced. The deduced amino acid sequence consists of 609 residues with molecular mass 68 kDa. An adjacent open reading frame is not transcribed under our experimental conditions. No evidence second related found. primary protein (P800 protein) shows high percentage identity to photosystem I in cysteine-containing loop, which putative binding site iron-sulfur FX preceding hydrophobic region. Our data imply homodimeric organization center. This fundamentally different most other centers, where composed two similar but nonidentical subunits.