Native FMO-reaction center supercomplex in green sulfur bacteria: an electron microscopy study
Language English Country Netherlands Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
26589322
DOI
10.1007/s11120-015-0205-y
PII: 10.1007/s11120-015-0205-y
Knihovny.cz E-resources
- Keywords
- Chlorosome, Electron microscopy, FMO (Fenna–Matthews–Olson protein), Green sulfur bacteria, Light-harvesting complex, Reaction center,
- MeSH
- Bacterial Proteins chemistry metabolism ultrastructure MeSH
- Chlorobi chemistry MeSH
- Cytoplasm chemistry MeSH
- Photosynthetic Reaction Center Complex Proteins chemistry metabolism MeSH
- Intracellular Membranes chemistry MeSH
- Light-Harvesting Protein Complexes chemistry metabolism ultrastructure MeSH
- Microscopy, Electron, Transmission MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Bacterial Proteins MeSH
- FMO bacteriochlorophyll protein, Bacteria MeSH Browser
- Photosynthetic Reaction Center Complex Proteins MeSH
- Light-Harvesting Protein Complexes MeSH
Chlorobaculum tepidum is a representative of green sulfur bacteria, a group of anoxygenic photoautotrophs that employ chlorosomes as the main light-harvesting structures. Chlorosomes are coupled to a ferredoxin-reducing reaction center by means of the Fenna-Matthews-Olson (FMO) protein. While the biochemical properties and physical functioning of all the individual components of this photosynthetic machinery are quite well understood, the native architecture of the photosynthetic supercomplexes is not. Here we report observations of membrane-bound FMO and the analysis of the respective FMO-reaction center complex. We propose the existence of a supercomplex formed by two reaction centers and four FMO trimers based on the single-particle analysis of the complexes attached to native membrane. Moreover, the structure of the photosynthetic unit comprising the chlorosome with the associated pool of RC-FMO supercomplexes is proposed.
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