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The architecture and function of the light-harvesting apparatus of purple bacteria: from single molecules to in vivo membranes.
- Source :
-
Quarterly reviews of biophysics [Q Rev Biophys] 2006 Aug; Vol. 39 (3), pp. 227-324. Date of Electronic Publication: 2006 Oct 12. - Publication Year :
- 2006
-
Abstract
- This review describes the structures of the two major integral membrane pigment complexes, the RC-LH1 'core' and LH2 complexes, which together make up the light-harvesting system present in typical purple photosynthetic bacteria. The antenna complexes serve to absorb incident solar radiation and to transfer it to the reaction centres, where it is used to 'power' the photosynthetic redox reaction and ultimately leads to the synthesis of ATP. Our current understanding of the biosynthesis and assembly of the LH and RC complexes is described, with special emphasis on the roles of the newly described bacteriophytochromes. Using both the structural information and that obtained from a wide variety of biophysical techniques, the details of each of the different energy-transfer reactions that occur, between the absorption of a photon and the charge separation in the RC, are described. Special emphasis is given to show how the use of single-molecule spectroscopy has provided a more detailed understanding of the molecular mechanisms involved in the energy-transfer processes. We have tried, with the help of an Appendix, to make the details of the quantum mechanics that are required to appreciate these molecular mechanisms, accessible to mathematically illiterate biologists. The elegance of the purple bacterial light-harvesting system lies in the way in which it has cleverly exploited quantum mechanics.
- Subjects :
- Amino Acid Sequence
Bacteriochlorophylls physiology
Carotenoids physiology
Energy Transfer
Light-Harvesting Protein Complexes physiology
Molecular Sequence Data
Proteobacteria physiology
Bacteriochlorophylls chemistry
Cell Membrane physiology
Light
Light-Harvesting Protein Complexes chemistry
Models, Molecular
Proteobacteria chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0033-5835
- Volume :
- 39
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Quarterly reviews of biophysics
- Publication Type :
- Academic Journal
- Accession number :
- 17038210
- Full Text :
- https://doi.org/10.1017/S0033583506004434