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Titolo:
On the influence of pigment-protein interactions on the energy transfer processes in photosynthetic membrane structures. 3. FMO complex of Chlorobiumtepidum at high pressure
Autore:
Klevanik, AV;
Indirizzi:
Russian Acad Sci, Inst Soil Sci & Photosynth, Pushchino 142292, Moscow Region, Russia Russian Acad Sci Pushchino Moscow Region Russia 142292 cow Region, Russia
Titolo Testata:
BIOLOGICHESKIE MEMBRANY
fascicolo: 4, volume: 16, anno: 1999,
pagine: 397 - 409
SICI:
0233-4755(199907/08)16:4<397:OTIOPI>2.0.ZU;2-7
Fonte:
ISI
Lingua:
RUS
Soggetto:
MATTHEWS-OLSON PROTEIN; PICOSECOND DYNAMICS; EXCITATION-ENERGY; REACTION CENTERS; PROSTHECOCHLORIS-AESTUARII; BACTERIOCHLOROPHYLL-ALPHA; RHODOBACTER-SPHAEROIDES; COHERENT MOTION; SPECTRAL HOLE; BACTERIA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Klevanik, AV Russian Acad Sci, Inst Soil Sci & Photosynth, Pushchino 142292, Moscow Region, Russia Russian Acad Sci Pushchino Moscow Region Russia 142292 ussia
Citazione:
A.V. Klevanik, "On the influence of pigment-protein interactions on the energy transfer processes in photosynthetic membrane structures. 3. FMO complex of Chlorobiumtepidum at high pressure", BIOL MEMB, 16(4), 1999, pp. 397-409

Abstract

The low-temperature absorption spectra of the Clorobium tepidum FMO bacteriochlorophyll-protein complex at various pressures have been calculated within the framework of the mini-exciton theory. The dependencies of the Q(y) transition energies of the monomeric pigments on pressure have been found by means of functional minimization. This functional includes the parametersof both theoretical and experimental absorption spectra at low temperatures and various pressures. The dependencies obtained are compared with those derived for the exciton transitions energies, which have been obtained by deconvoluting absorption spectra with seven Gaussian components at each pressure. The pressure increase has been shown to result in the increased coupling energy between both the pigment molecules themselves and pigments and amino acid residues. The greatest and smallest responses to the increased pressure have been revealed to show the pigment molecules liganded by histidines and water molecule, respectively. The couplings of Bchl molecules with the surrounding amino acid residues have been shown to change both the exciton delocalization index and exciton distribution between the pigment molecules within the protein Subunit; the increased pressure does not change significantly these parameters.

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Documento generato il 25/11/20 alle ore 03:53:50