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Pigment–protein architecture in the light‐harvesting antenna complexes of purple bacteria: does the crystal structure reflect the native pigment–protein arrangement?
Author(s) -
Leupold D,
Voigt B,
Beenken W,
Stiel H
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01892-5
Subject(s) - purple bacteria , rhodobacter sphaeroides , pigment , photosynthetic reaction centre , bacteriochlorophyll , rhodospirillaceae , chemistry , antenna (radio) , absorption (acoustics) , light harvesting complex , crystallography , photochemistry , materials science , optics , photosynthesis , electron transfer , physics , photosystem ii , organic chemistry , biochemistry , telecommunications , computer science
Structural analysis of crystallized peripheral (LH2) and core antenna complexes (LH1) of purple bacteria has revealed circular aggregates of high rotational symmetry (C 8 , C 9 and C 16 , respectively). Quantum‐chemical calculations indicate that in particular the waterwheel‐like arrangements of pigments should show characteristic structure‐sensitive spectroscopic behavior in the near infrared absorption region. Laser‐spectroscopic data obtained with non‐crystallized, isolated LH2 of Rhodospirillum molischianum are in line with a highly symmetric (C 8 ) circular aggregate, but deviations have been found for LH2 of Rhodobacter sphaeroides and Rhodopseudomonas acidophila . For both the latter, C‐shaped incomplete circular aggregates (as seen only recently in electron micrographs of crystallized LH1–reaction center complexes) may be a suitable preliminary model.