Structural differences in chlorosomes fromChloroflexus aurantiacusgrown under different conditions support the BChlc-binding function of the 5.7 kDa polypeptide

Abstract

Structurally different chlorosomes were isolated from the green photosynthetic bacterium Chloroflexus aurantiacus grown under different conditions. They were analysed with respect to variable pigment-protein stoichiometries in view of the presumed BChI c-binding function of the 5.7 kDa chlorosome polypeptide. Under high-light conditions on substrate-limited growth medium the pigment-protein ratio of isolated chlorosomes was several times lower than under low-light conditions on complex medium. Proteolytic degradation of the 5.7 kDa polypeptide in high-light chlorosomes led to a 60% decrease of the absorbance at 740 nm. The CD spectrum of high-light chlorosomes exhibited a sixfold lower relative intensity at 740 nm (ΔA/A ₇₄₀) than low-light chlorosomes, but it showed a fivefold increase in intensity upon degradation of the 5.7 kDa polypeptide compared to a twofold increase in low-light chlorosomes. It seems probable that BChl c in the chlorosomes is present as oligomers bound to the 5.7 kDa polypeptide. Our data suggest further that compared to low-light chlorosomes smaller oligomers or single BChl c molecules are bound to the 5.7 kDa polypeptide in high-light chlorosomes resulting in lower rotational strength.