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How Well Does the Hole-Burning Action Spectrum Represent the Site-Distribution Function of the Lowest-Energy State in Photosynthetic Pigment-Protein Complexes?

Author(s): Zazubovich V, Jankowiak R

J Phys Chem B. 2019 Jul 02;: Authors: Zazubovich V, Jankowiak R

Article GUID: 31265294
Low-temperature protein dynamics of the B800 molecules in the LH2 light-harvesting complex: spectral hole burning study and comparison with single photosynthetic complex spectroscopy.

Author(s): Grozdanov D, Herascu N, Reinot T, Jankowiak R, Zazubovich V

J Phys Chem B. 2010 Mar 18;114(10):3426-38 Authors: Grozdanov D, Herascu N, Reinot T, Jankowiak R, Zazubovich V

Article GUID: 20166717
Effects of the distributions of energy or charge transfer rates on spectral hole burning in pigment-protein complexes at low temperatures.

Author(s): Herascu N, Ahmouda S, Picorel R, Seibert M, Jankowiak R, Zazubovich V

J Phys Chem B. 2011 Dec 22;115(50):15098-109 Authors: Herascu N, Ahmouda S, Picorel R, Seibert M, Jankowiak R, Zazubovich V

Article GUID: 22046956
Spectral hole burning, recovery, and thermocycling in chlorophyll-protein complexes: distributions of barriers on the protein energy landscape.

Author(s): Najafi M, Herascu N, Seibert M, Picorel R, Jankowiak R, Zazubovich V

J Phys Chem B. 2012 Sep 27;116(38):11780-90 Authors: Najafi M, Herascu N, Seibert M, Picorel R, Jankowiak R, Zazubovich V

Article GUID: 22957798
Modeling of various optical spectra in the presence of slow excitation energy transfer in dimers and trimers with weak interpigment coupling: FMO as an example.

Author(s): Herascu N, Kell A, Acharya K, Jankowiak R, Blankenship RE, Zazubovich V

J Phys Chem B. 2014 Feb 27;118(8):2032-40 Authors: Herascu N, Kell A, Acharya K, Jankowiak R, Blankenship RE, Zazubovich V

Article GUID: 24506338
On the Controversial Nature of the 825 nm Exciton Band in the FMO Protein Complex.

Author(s): Kell A, Acharya K, Zazubovich V, Jankowiak R

J Phys Chem Lett. 2014 Apr 17;5(8):1450-6 Authors: Kell A, Acharya K, Zazubovich V, Jankowiak R

Article GUID: 26269993
On the Conflicting Estimations of Pigment Site Energies in Photosynthetic Complexes: A Case Study of the CP47 Complex.

Author(s): Reinot T, Chen J, Kell A, Jassas M, Robben KC, Zazubovich V, Jankowiak R

Anal Chem Insights. 2016;11:35-48 Authors: Reinot T, Chen J, Kell A, Jassas M, Robben KC, Zazubovich V, Jankowiak R

Article GUID: 27279733
Title:On the Controversial Nature of the 825 nm Exciton Band in the FMO Protein Complex.
Authors:Kell A,  Acharya K,  Zazubovich V,  Jankowiak R
Link:https://www.ncbi.nlm.nih.gov/pubmed/26269993?dopt=Abstract
Category:J Phys Chem Lett
PMID:26269993
Dept Affiliation: PHYSICS
1 §Department of Physics, Concordia University, Montreal H4B 1R6, Quebec, Canada.

Description:

On the Controversial Nature of the 825 nm Exciton Band in the FMO Protein Complex.

J Phys Chem Lett. 2014 Apr 17;5(8):1450-6

Authors: Kell A, Acharya K, Zazubovich V, Jankowiak R

Abstract

The nature of the low-energy 825 nm band of the Fenna-Matthews-Olson (FMO) protein complex from Chlorobaculum tepidum at 5 K is discussed. It is shown, using hole-burning (HB) spectroscopy and excitonic calculations, that the 825 nm absorption band of the FMO trimer cannot be explained by a single electronic transition or overlap of electronic transitions of noninteracting pigments. To explain the shape of emission and nonresonant HB spectra, downward uncorrelated excitation energy transfer (EET) between trimer subunits should be taken into account. Modeling studies reveal the presence of three sub-bands within the 825 nm band, in agreement with nonresonant HB and emission spectra. We argue that after light induced coherences vanish, uncorrelated EET between the lowest exciton levels of each monomer takes place. HB induced spectral shifts provide a new insight on the energy landscape of the FMO protein.

PMID: 26269993 [PubMed]