B800-->B850 energy transfer mechanism in bacterial LH2 complexes investigated by B800 pigment exchange

Biophys J. 2000 May;78(5):2590-6. doi: 10.1016/S0006-3495(00)76803-2.

Abstract

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 approximately 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins*
  • Biophysical Phenomena
  • Biophysics
  • Electrochemistry
  • Energy Transfer
  • Light-Harvesting Protein Complexes*
  • Photosynthetic Reaction Center Complex Proteins / chemistry*
  • Rhodopseudomonas / chemistry
  • Spectrophotometry

Substances

  • B800-850 light-harvesting complex, bacteria
  • Bacterial Proteins
  • Light-Harvesting Protein Complexes
  • Photosynthetic Reaction Center Complex Proteins