Keyword search (4,163 papers available)

"Jankowiak R" Authored Publications:

Title Authors PubMed ID
1 High-Resolution Frequency-Domain Spectroscopic and Modeling Studies of Photosystem I (PSI), PSI Mutants and PSI Supercomplexes Zazubovich V; Jankowiak R; 38612659
PHYSICS
2 Frequency-Domain Spectroscopic Study of the Photosystem I Supercomplexes, Isolated IsiA Monomers, and the Intact IsiA Ring Reinot T; Khmelnitskiy A; Zazubovich V; Toporik H; Mazor Y; Jankowiak R; 36065077
PHYSICS
3 How Well Does the Hole-Burning Action Spectrum Represent the Site-Distribution Function of the Lowest-Energy State in Photosynthetic Pigment-Protein Complexes? Zazubovich V, Jankowiak R 31265294
CHEMISTRY
4 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. Grozdanov D, Herascu N, Reinot T, Jankowiak R, Zazubovich V 20166717
PHYSICS
5 Effects of the distributions of energy or charge transfer rates on spectral hole burning in pigment-protein complexes at low temperatures. Herascu N, Ahmouda S, Picorel R, Seibert M, Jankowiak R, Zazubovich V 22046956
PHYSICS
6 Spectral hole burning, recovery, and thermocycling in chlorophyll-protein complexes: distributions of barriers on the protein energy landscape. Najafi M, Herascu N, Seibert M, Picorel R, Jankowiak R, Zazubovich V 22957798
PHYSICS
7 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. Herascu N, Kell A, Acharya K, Jankowiak R, Blankenship RE, Zazubovich V 24506338
PHYSICS
8 On the Controversial Nature of the 825 nm Exciton Band in the FMO Protein Complex. Kell A, Acharya K, Zazubovich V, Jankowiak R 26269993
PHYSICS
9 On the Conflicting Estimations of Pigment Site Energies in Photosynthetic Complexes: A Case Study of the CP47 Complex. Reinot T, Chen J, Kell A, Jassas M, Robben KC, Zazubovich V, Jankowiak R 27279733
PHYSICS

 

Title:On the Controversial Nature of the 825 nm Exciton Band in the FMO Protein Complex.
Authors:Kell AAcharya KZazubovich VJankowiak R
Link:https://www.ncbi.nlm.nih.gov/pubmed/26269993?dopt=Abstract
Publication:
Keywords:
PMID:26269993 Category:J Phys Chem Lett Date Added:2019-06-04
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]





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