Literature DB >> 938647

Exciton interaction among chlorophyll molecules in bacteriochlorophyllaproteins and bacteriochlorophyllareaction center complexes from green bacteria.

J M Olson, B Ke, K H Thompson.   

Abstract

Absorption and CD spectra of bacteriochlorophyll a proteins and bacteriochlorophyll a reaction center complexes from two strains of Chlorobium limicola were recorded at 77 degrees K. Visual inspection showed that the Qy-band of chlorophyll in either protein was split into at least five components. Analysis of the spectra in terms of asymmetric Gaussian component pairs by means of computer program GAMET showed that six components are necessary to fit the spectra from strain 2K. These six components are ascribed to an exciton interaction between the seven bacteriochlorophyll a molecules in each subunit. The clear difference between the exciton splitting in the two bacteriochlorophyll a proteins shows that the arrangement of the chlorophyll molecules in each subunit must be slightly different. The spectra for the bacteriochlorophyll a reaction center complexes have a component at 834 nm (absorption) and 832 nm (CD) which does not appear in the spectra of the bacteriochlorophyll a proteins. The new component is ascribed to a reaction center complex which is combined with bacteriochlorophyll a proteins to form the bacteriochlorophyll a reaction center complex. The complete absorption (or CD) spectrum for a given bacteriochlorophyll a reaction center complex can be described to a first approximation in terms of the absorption (or CD) spectrum for the corresponding bacteriochlorophyll a protein plus the new component ascribed to the reaction center complex.

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Year:  1976        PMID: 938647     DOI: 10.1016/0005-2728(76)90028-1

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  17 in total

1.  Comparison of bacteriochlorophyll a-proteins from two green bacteria.

Authors:  J M Olson; E K Shaw; F M Englberger
Journal:  Biochem J       Date:  1976-12-01       Impact factor: 3.857

2.  The quantitative relationship between structure and polarized spectroscopy in the FMO complex of Prosthecochloris aestuarii: refining experiments and simulations.

Authors:  Markus Wendling; Milosz A Przyjalgowski; Demet Gülen; Simone I E Vulto; Thijs J Aartsma; Rienk van Grondelle; Herbert van Amerongen
Journal:  Photosynth Res       Date:  2002       Impact factor: 3.573

3.  The FMO Protein.

Authors:  John M Olson
Journal:  Photosynth Res       Date:  2004       Impact factor: 3.573

4.  Giant circular dichroism of high molecular weight chlorophyllide-apomyoglobin complexes.

Authors:  R M Pearlstein; R C Davis; S L Ditson
Journal:  Proc Natl Acad Sci U S A       Date:  1982-01       Impact factor: 11.205

5.  Bacteriochlorophyll electronic transition moment directions in bacteriochlorophyll a-protein.

Authors:  R M Pearlstein; R P Hemenger
Journal:  Proc Natl Acad Sci U S A       Date:  1978-10       Impact factor: 11.205

6.  Organization of Chlorophyll a in the Light-Harvesting Chlorophyll a/b Protein Complex as Shown by Circular Dichroism : Liquid Crystal-Like Domains.

Authors:  A Faludi-Dániel; L A Mustárdy
Journal:  Plant Physiol       Date:  1983-09       Impact factor: 8.340

7.  The structural basis for the difference in absorbance spectra for the FMO antenna protein from various green sulfur bacteria.

Authors:  Dale E Tronrud; Jianzhong Wen; Leslie Gay; Robert E Blankenship
Journal:  Photosynth Res       Date:  2009-05-13       Impact factor: 3.573

8.  Low-temperature spectroscopy of isolated FMO-protein and a membrane-free reaction center complex from the green sulfur bacteriumChlorobium tepidum.

Authors:  M Miller; R P Cox; J M Olson
Journal:  Photosynth Res       Date:  1994-07       Impact factor: 3.573

9.  Pump-probe anisotropies of Fenna-Matthews-Olson protein trimers from Chlorobium tepidum: a diagnostic for exciton localization?

Authors:  S Savikhin; D R Buck; W S Struve
Journal:  Biophys J       Date:  1997-10       Impact factor: 4.033

10.  Ultrafast absorption difference spectra of the Fenna-Matthews-Olson protein at 19 K: experiment and simulations.

Authors:  D R Buck; S Savikhin; W S Struve
Journal:  Biophys J       Date:  1997-01       Impact factor: 4.033

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