Discrepancy between experimental and theoretical excitation transfer rates in LH2 bacteriochlorophyll-protein complexes of purple bacteria

• Published in: European biophysics journal 2008-02, Vol.37 (2), p.143-151
• Main Author: Borisov, A. Y.
• Format: Article
• Language: English
• Subjects: Bacteria; Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Bacteriochlorophylls - chemistry; Bacteriochlorophylls - metabolism; Biochemistry; Biological and Medical Physics; Biomedical and Life Sciences; Biophysics; Cell Biology; Crystallization; Electrons; Kinetics; Life Sciences; Light-Harvesting Protein Complexes - chemistry; Light-Harvesting Protein Complexes - metabolism; Membrane Biology; Models, Biological; Nanotechnology; Neurobiology; Original Paper; Proteins; Reproducibility of Results; Rhodopseudomonas - metabolism; Time Factors
• ISSN: 0175-7571; 1432-1017
• DOI: 10.1007/s00249-007-0200-0

Discrepancy is revealed between the values of excitation transfer times measured experimentally, and those calculated, for the atomic structures of B800 → B850 bacteriochlorophylls within the LH2 light-harvesting pigment–protein complex of the purple bacterium Rhodopseudomonas acidophila . The value 2.9–3.2 ps for the B800 → B850 excitation transfer, calculated on the basis of atomic structure of LH2, is about 4-times longer than that measured for this bacterium (0.7 ps). This discrepancy appears common in at least two purple bacteria. Possible sources responsible for this discrepancy are discussed. It may either signify some drawback/s/ in our notions about the precise in vivo structure of LH2 complexes, for example, possible changes of LH2 structure during crystallization, or it may reflect our ignorance of some mechanisms involved in excitation migration.