4.5 Article

Energy transfer in an LH4-like light harvesting complex from the aerobic purple photosynthetic bacterium Roseobacter denitrificans

Journal

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
Volume 1807, Issue 5, Pages 518-528

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbabio.2011.03.004

Keywords

LH4; LH2; Carotenoids; Bacteriochlorophyll; Transient absorption; Light harvesting

Funding

  1. U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-SC 0001035]
  2. National Science Foundation [MCB-0913022]
  3. University of Connecticut Research Foundation
  4. Div Of Molecular and Cellular Bioscience
  5. Direct For Biological Sciences [0913022] Funding Source: National Science Foundation

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A peripheral light-harvesting complex from the aerobic purple bacterium Roseobacter (R.) denitrificans was purified and its photophysical properties characterized. The complex contains two types of pigments, bacteriochlorophyll (BChl) a and the carotenoid (Car) spheroidenone and possesses unique spectroscopic properties. It appears to lack the B850 bacteriochlorophyll a Q(y) band that is typical for similar light-harvesting complex 2 antennas. Circular dichroism and low temperature steady-state absorption spectroscopy revealed that the B850 band is present but is shifted significantly to shorter wavelengths and overlaps with the B800 band at room temperature. Such a spectral signature classifies this protein as a member of the light-harvesting complex 4 class of peripheral light-harvesting complexes, along with the previously known light-harvesting complex 4 from Rhodopseudomonas palustris. The influence of the spectral change on the light-harvesting ability was studied using steady-state absorption, fluorescence, circular dichroism, femtosecond and microsecond time-resolved absorption and time-resolved fluorescence spectroscopies. The results were compared to the properties of the similar (in pigment composition) light-harvesting complex 2 from aerobically grown Rhodobacter sphaeroides and are understood within the context of shared similarities and differences and the putative influence of the pigments on the protein structure and its properties. (C) 2011 Elsevier B.V. All rights reserved.

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