Femtosecond probe of structural analogies between chlorosomes and bacteriochlorophyll c aggregates.
Bacteriochlorophyll c pigments extracted from light harvesting chlorosomes in green photosynthetic bacteria are known to self-assemble into aggregates whose electronic spectroscopy resembles that of intact chlorosomes. Femtosecond optical experiments reveal that the chlorosomes and their reconstituted aggregates exhibit closely analogous internal energy transfer kinetics and exciton state evolution. These comparisons furnish compelling new evidence that proteins do not exert a major local role in the BChl c antenna pigment organization of intact chlorosomes.
Ames Laboratory, U.S. Department of Energy, Iowa, USA.
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van Noort
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D001419:Bacteria / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D001429:Bacteriochlorophylls; D007700:Kinetics; D045342:Light-Harvesting Protein Complexes; D015388:Organelles / Q000378:metabolism; D010788:Photosynthesis; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000378:metabolism; D012242:Rhodobacter sphaeroides / Q000378:metabolism; D016999:Sulfur-Reducing Bacteria / Q000378:metabolism; D013997:Time Factors
D001426:Bacterial Proteins; D001429:Bacteriochlorophylls; D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; C002084:bacteriochlorophyll c