Pigment–protein architecture in the light-harvesting antenna complexes of purple bacteria: does the crystal structure reflect the native pigment–protein arrangement?
| Autor: | Wichard J. D. Beenken, B. Voigt, Holger Stiel, Dieter Leupold |
|---|---|
| Jazyk: | angličtina |
| Předmět: |
food.ingredient
Protein Conformation Photosynthetic Reaction Center Complex Proteins Biophysics Light-Harvesting Protein Complexes Crystal structure Rhodobacter sphaeroides Photosynthetic antenna complex Photochemistry Biochemistry Purple bacteria Pigment food Rhodospirillum molischianum Bacterial Proteins Structural Biology Genetics Molecular Biology Rhodopseudomonas acidophila Rhodospirillum Spectroscopy Near-Infrared biology Chemistry Circular aggregate Cell Biology Pigments Biological Rhodopseudomonas biology.organism_classification Crystallography visual_art Electron micrographs visual_art.visual_art_medium Light-Harvesting Antenna Complexes |
| Zdroj: | FEBS Letters. (2-3):73-78 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/S0014-5793(00)01892-5 |
| Popis: | Structural analysis of crystallized peripheral (LH2) and core antenna complexes (LH1) of purple bacteria has revealed circular aggregates of high rotational symmetry (C8, C9 and C16, 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 (C8) 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. |
| Databáze: | OpenAIRE |
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