Structure of the Antenna Complexes from Purple Bacteria as Seen from Resonance Raman Spectroscopy
Since 1984, X-ray diffraction studies of crystallized bacterial reaction centers (RC) allowed the structure of these protein-pigment complexes to be solved with an atomic resolution [1–2]. By contrast, none of the several attempts to crystallyse light-harvesting complexes of purple bacteria (Rhodospirillales) had resulted in highly diffracting crystals until only very recently. Only this year has there been a report of 3.5 angströms diffracting crystals , but no structural model has yet been obtained from the diffraction patterns. On the other hand, a large body of information has been obtained by different biochemical and biophysical methods (see below). Resonance Raman (RR) spectroscopy is still, currently, the only method capable of providing direct information about the interactions between the bacteriochlorophyll (BChl) molecules present in these complexes and their local, proteic environments , thus giving detailed information on the structures of the BChl host sites within the protein. In this work, we have tried to fit the RR results and the conclusions drawn from other methods, in order to build models of the membrane-embedded parts of the light-harvesting complexes.
KeywordsPurple Bacterium Resonance Raman Resonance Raman Spectrum Primary Electron Donor Resonance Raman Spectroscopy
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