B800→B850 Energy Transfer Mechanism in Bacterial LH2 Complexes Investigated by B800 Pigment Exchange

• Published in: Biophysical journal 2000-05, Vol.78 (5), p.2590-2596
• Main Authors: Herek, J.L., Fraser, N.J., Pullerits, T., Martinsson, P., Polívka, T., Scheer, H., Cogdell, R.J., Sundström, V.
• Format: Article
• Language: English
• Subjects: Bacteria; Bacterial Proteins; Biophysical Phenomena; Biophysics; Electrochemistry; Energy Transfer; Light-Harvesting Protein Complexes; Molecular biology; Photosynthetic Reaction Center Complex Proteins - chemistry; Rhodopseudomonas - chemistry; Spectrophotometry
• ISSN: 0006-3495; 1542-0086
• DOI: 10.1016/S0006-3495(00)76803-2

Femtosecond transient absorption measurements were performed on native and a series of reconstituted LH2 complexes from Rhodopseudomonas acidophila 10050 at room temperature. The reconstituted complexes contain chemically modified tetrapyrrole pigments in place of the native bacteriochlorophyll a-B800 molecules. The spectral characteristics of the modified pigments vary significantly, such that within the B800 binding sites the B800 Q y absorption maximum can be shifted incrementally from 800 to 670 nm. As the spectral overlap between the B800 and B850 Q y bands decreases, the rate of energy transfer (as determined by the time-dependent bleaching of the B850 absorption band) also decreases; the measured time constants range from 0.9 ps (bacteriochlorophyll a in the B800 sites, Q y absorption maximum at 800 nm) to 8.3 ps (chlorophyll a in the B800 sites, Q y absorption maximum at 670 nm). This correlation between energy transfer rate and spectral blue-shift of the B800 absorption band is in qualitative agreement with the trend predicted from Förster spectral overlap calculations, although the experimentally determined rates are ∼5 times faster than those predicted by simulations. This discrepancy is attributed to an underestimation of the electronic coupling between the B800 and B850 molecules.