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Calculation of pigment transition energies in the FMO protein

From simplicity to complexity and back

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An Erratum to this article was published on 31 October 2007

An Erratum to this article was published on 31 October 2007

Abstract

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.

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Notes

  1. We use different widths for the seven pigments. Pigments 1, 3, 4: fwhm = 60 cm−1; Pigment 2: fwhm = 100  cm−1; Pigments 5–7: fwhm = 120 cm−1. This empirical assignment is based on the assumption that those BChls, which according to the crystal structure have more water molecules bound in their vicinity, should have a larger disorder because of the structural heterogeneity of the water molecules.

  2. A value of R c = 5 Å is used, that was determined from transient spectra of photosystem II reaction centers in Renger and Marcus (2002b). The stationary spectra calculated here do not depend critically on this value.

  3. For BChla in polystyrene (ɛ = 2.6), a value \(|\Updelta{\mathbf{d}}|/f\) of 2–3 was reported (Lockhart and Boxer 1987). Using the empty cavity factor f = 3ɛ/(2ɛ + 1), then results in \(|\Updelta{\mathbf{d}}|=1.6-2.4\).

  4. These water molecules are the hydrogen bond donor to the 3-acetyl group of BChl 1, the axial ligand to the Mg atom of BChl 2, and two water molecules bridging the side chains of Asp 234 and Ser 235 via H-bonds.

  5. The close proximity of one water molecule to the 131-keto group of BChl 5 suggests formation of an H-bond there, but in our structural model this water molecule is oriented towards the negatively charged Asp 234, so that no H-bond is formed. Turning the water molecule towards the 131-keto group of BChl 5 results in a moderate red shift of ≈ 50 cm−1.

Abbreviations

BChl:

Bacteriochlorophyll

CD:

Circular dichroism

CDC:

Charge density coupling

FMO:

Fenna–Matthews–Olson

LD:

Linear dichroism

OD:

Absorption

PBQC:

Poisson–Boltzmann quantum chemistry

PCD:

Point charge-dipole

PPC:

Pigment-protein complex

RMSD:

Root mean square deviation

TrEsp:

Transition charge from electrostatic potential

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Acknowledgements

We would like to acknowledge support by the Deutsche Forschungsgemeinschaft through Emmy-Noether research grant RE 1610 and through the Sonderforschungsbereich 498, TP A7.

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Authors and Affiliations

  1. Institut für Chemie und Biochemie, Freie Universität Berlin, Takustrasse 6, Berlin, 14195, Germany

    Julian Adolphs, Frank Müh, Mohamed El-Amine Madjet & Thomas Renger

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  1. Julian Adolphs
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  2. Frank Müh
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  3. Mohamed El-Amine Madjet
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  4. Thomas Renger
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Correspondence to Thomas Renger.

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An erratum to this article can be found at http://dx.doi.org/10.1007/s11120-007-9276-8

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Adolphs, J., Müh, F., Madjet, M.EA. et al. Calculation of pigment transition energies in the FMO protein. Photosynth Res 95, 197–209 (2008). https://doi.org/10.1007/s11120-007-9248-z

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