Single-Molecule Spectroscopy Reveals that Individual Low-Light LH2 Complexes from Rhodopseudomonas palustris 2.1.6. Have a Heterogeneous Polypeptide Composition

AUTOR(ES)

Brotosudarmo, Tatas H.P.

FONTE

The Biophysical Society

RESUMO

Rhodopseudomonas palustris belongs to the group of purple bacteria that have the ability to produce LH2 complexes with unusual absorption spectra when they are grown at low-light intensity. This ability is often related to the presence of multiple genes encoding the antenna apoproteins. Here we report, for the first time to our knowledge, direct evidence that individual low-light LH2 complexes have a heterogeneous αβ-apoprotein composition that modulates the site energies of Bchl a molecules, producing absorption bands at 800, 820, and 850 nm. The arrangement of the Bchl a molecules in the “tightly coupled ring” can be modeled by nine αβ-Bchls dimers, such that the Bchls bound to six αβ-pairs have B820-like site energies and the remaining Bchl a molecules have B850-like site energies. Furthermore, the experimental data can only be satisfactorily modeled when these six αβ-pairs with B820 Bchl a molecules are distributed such that the symmetry of the assembly is reduced to C3. It is also clear from the measured single-molecule spectra that the energies of the electronically excited states in the mixed B820/850 ring are mainly influenced by diagonal disorder.

Documentos Relacionados

• Multiparameter single-molecule fluorescence spectroscopy reveals heterogeneity of HIV-1 reverse transcriptase:primer/template complexes
• Single-molecule microscopy on model membranes reveals anomalous diffusion.
• Imaging of single-molecule translocation through nuclear pore complexes
• Site-specific labeling of the ribosome for single-molecule spectroscopy
• Single-molecule fluorescence spectroscopy of enzyme conformational dynamics and cleavage mechanism