A quantum mechanical analysis of the light-harvesting complex 2 from purple photosynthetic bacteria. Insights into the electrostatic effects of transmembrane helices

Details A quantum mechanical analysis of the light-harvesting complex 2 from purple photosynthetic bacteria. Insights into the electrostatic effects of transmembrane helices A quantum mechanical analysis of the light-harvesting complex 2 from purple photosynthetic bacteria. Insights into the electrostatic effects of transmembrane helices

2010-06-25

arxiv.org/abs/1006.4911v1

BioSystems 103 (2011) 132-137

Biology

Quantitative Biology

Biomolecules

14 pages, 7 figures

Scientific paper

10.1016/j.biosystems.2010.08.006

We perform a quantum mechanical study of the peptides that are part of the LH2 complex from Rhodopseudomonas acidophila, a non-sulfur purple bacteria that has the ability of producing chemical energy from photosynthesis. The electronic structure calculations indicate that the transmembrane helices of these peptides are characterized by dipole moments with a magnitude of ~150 D. When the full nonamer assembly made of eighteen peptides is considered, then a macrodipole of magnitude 704 D is built up from the vector sum of each monomer dipole. The macrodipole is oriented normal to the membrane plane and with the positive tip toward the cytoplasm thereby indicating that the electronic charge of the protein scaffold is polarized toward the periplasm. The results obtained here suggest that the asymmetric charge distribution of the protein scaffold contributes an anisotropic electrostatic environment which differentiates the absorption properties of the bacteriochlorophyll pigments, B800 and B850, embedded in the LH2 complex.

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