Plant photosystem I design in the light of evolution
- PMID: 19446520
- DOI: 10.1016/j.str.2009.03.006
Plant photosystem I design in the light of evolution
Abstract
Photosystem I (PSI) is a membrane protein complex that catalyzes sunlight-driven transmembrane electron transfer as part of the photosynthetic machinery. Photosynthetic organisms appeared on the Earth about 3.5 billion years ago and provided an essential source of potential energy for the development of life. During the course of evolution, these primordial organisms were phagocytosed by more sophisticated eukaryotic cells, resulting in the evolvement of algae and plants. Despite the extended time interval between primordial cyanobacteria and plants, PSI has retained its fundamental mechanism of sunlight conversion. Being probably the most efficient photoelectric apparatus in nature, PSI operates with a quantum efficiency close to 100%. However, adapting to different ecological niches necessitated structural changes in the PSI design. Based on the recently solved structure of plant PSI, which revealed a complex of 17 protein subunits and 178 prosthetic groups, we analyze the evolutionary development of PSI. In addition, some aspects of PSI structure determination are discussed.
Similar articles
-
Evolution of photosystem I - from symmetry through pseudo-symmetry to asymmetry.FEBS Lett. 2004 Apr 30;564(3):274-80. doi: 10.1016/S0014-5793(04)00360-6. FEBS Lett. 2004. PMID: 15111109 Review.
-
Light harvesting in photosystem I supercomplexes.Biochemistry. 2006 Jan 17;45(2):331-45. doi: 10.1021/bi051932o. Biochemistry. 2006. PMID: 16401064 Review.
-
The structure of photosystem I and evolution of photosynthesis.Bioessays. 2005 Sep;27(9):914-22. doi: 10.1002/bies.20278. Bioessays. 2005. PMID: 16108066 Review.
-
Photosynthetic acclimation: structural reorganisation of light harvesting antenna--role of redox-dependent phosphorylation of major and minor chlorophyll a/b binding proteins.FEBS J. 2008 Mar;275(6):1056-68. doi: 10.1111/j.1742-4658.2008.06262.x. FEBS J. 2008. PMID: 18318833 Review.
-
CP43-like chlorophyll binding proteins: structural and evolutionary implications.Trends Plant Sci. 2006 Mar;11(3):152-8. doi: 10.1016/j.tplants.2006.01.007. Epub 2006 Feb 13. Trends Plant Sci. 2006. PMID: 16473546 Review.
Cited by
-
Structure determination and improved model of plant photosystem I.J Biol Chem. 2010 Jan 29;285(5):3478-86. doi: 10.1074/jbc.M109.072645. Epub 2009 Nov 18. J Biol Chem. 2010. PMID: 19923216 Free PMC article.
-
Cofactor-specific photochemical function resolved by ultrafast spectroscopy in photosynthetic reaction center crystals.Proc Natl Acad Sci U S A. 2012 Mar 27;109(13):4851-6. doi: 10.1073/pnas.1116862109. Epub 2012 Mar 12. Proc Natl Acad Sci U S A. 2012. PMID: 22411820 Free PMC article.
-
Isolation of novel PSII-LHCII megacomplexes from pea plants characterized by a combination of proteomics and electron microscopy.Photosynth Res. 2016 Dec;130(1-3):19-31. doi: 10.1007/s11120-016-0216-3. Epub 2016 Jan 9. Photosynth Res. 2016. PMID: 26749480
-
CO-EXPRESSED WITH PSI ASSEMBLY1 (CEPA1) is a photosystem I assembly factor in Arabidopsis.Plant Cell. 2024 Oct 3;36(10):4179-4211. doi: 10.1093/plcell/koae042. Plant Cell. 2024. PMID: 38382089 Free PMC article.
-
PsbP-domain protein1, a nuclear-encoded thylakoid lumenal protein, is essential for photosystem I assembly in Arabidopsis.Plant Cell. 2012 Dec;24(12):4992-5006. doi: 10.1105/tpc.112.106542. Epub 2012 Dec 7. Plant Cell. 2012. PMID: 23221595 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources