Calculation of pigment transition energies in the FMO protein: from simplicity to complexity and back.
The Fenna-Matthews-Olson (FMO) protein of green sulfur bacteria represents an important model protein for the study of elementary pigment-protein couplings. We have previously used a simple approach [Adolphs and Renger (2006) Biophys J 91:2778-2797] to study the shift in local transition energies (site energies) of the FMO protein of Prosthecochloris aestuarii by charged amino acid residues, assuming a standard protonation pattern of the titratable groups. Recently, we have found strong evidence that besides the charged amino acids also the neutral charge density of the protein is important, by applying a combined quantum chemical/electrostatic approach [Müh et al. (2007) Proc Natl Acad Sci USA, in press]. Here, we extract the essential parts from this sophisticated method to obtain a relatively simple method again. It is shown that the main contribution to the site energy shifts is due to charge density coupling (CDC) between the pigments and their pigment, protein and water surroundings and that polarization effects for qualitative considerations can be approximated by screening the Coulomb coupling by an effective dielectric constant.
Adolphs
Julia
J
Institut für Chemie und Biochemie, Freie Universität Berlin, Takustrasse 6, Berlin, 14195, Germany.
Müh
Frank
F
Madjet
Mohamed El-Amine
Mel-A
Renger
Thomas
T
D001426:Bacterial Proteins / Q000378:metabolism*; D019414:Chlorobi / Q000378:metabolism*; D005583:Fourier Analysis; D045342:Light-Harvesting Protein Complexes / Q000378:metabolism*; D008954:Models, Biological; D010860:Pigments, Biological / Q000378:metabolism*; D013057:Spectrum Analysis / Q000379:methods
D001426:Bacterial Proteins; C086320:FMO bacteriochlorophyll protein, Bacteria; D045342:Light-Harvesting Protein Complexes; D010860:Pigments, Biological