| 词条 | Phycobilisome | ||
| 释义 |
| Symbol = Phycobilisome | Name = Phycobilisome protein | image = Phycobilisome structure.jpg | width = | caption = The layout of protein subunits in a phycobilisome. | Pfam= PF00502 | InterPro= [https://www.ebi.ac.uk/interpro/entry/IPR012128?q=phycocyanin IPR012128] | SMART= | Prosite = | SCOP = 1cpc | TCDB = | OPM family= | OPM protein= }} Phycobilisomes are light harvesting antennae of photosystem II in cyanobacteria, red algae and glaucophytes. General structurePhycobilisomes are protein complexes (up to 600 polypeptides) anchored to thylakoid membranes. They are made of stacks of chromophorylated proteins, the phycobiliproteins, and their associated linker polypeptides. Each phycobilisome consists of a core made of allophycocyanin, from which several outwardly oriented rods made of stacked disks of phycocyanin and (if present) phycoerythrin(s) or phycoerythrocyanin. The spectral property of phycobiliproteins are mainly dictated by their prosthetic groups, which are linear tetrapyrroles known as phycobilins including phycocyanobilin, phycoerythrobilin, phycourobilin and phycobiliviolin. The spectral properties of a given phycobilin is influenced by its protein environment. FunctionEach phycobiliprotein has a specific absorption and fluorescence emission maximum in the visible range of light. Therefore, their presence and the particular arrangement within the phycobilisomes allow absorption and unidirectional transfer of light energy to chlorophyll a of the photosystem II. In this way, the cells take advantage of the available wavelengths of light (in the 500-650 nm range), which are inaccessible to chlorophyll, and utilize their energy for photosynthesis. This is particularly advantageous deeper in the water column, where light with longer wavelengths is less transmitted and therefore less available directly to chlorophyll. The geometrical arrangement of a phycobilisome is very elegant{{how|date=November 2016}} and results in 95% efficiency of energy transfer.[1] Evolution and diversityThere are many variations to the general phycobilisomes structure. Their shape can be hemidiscoidal (in cyanobacteria) or hemiellipsoidal (in red algae). Species lacking phycoerythrin have at least two disks of phycocyanin per rod, which is sufficient for maximum photosynthesis.[2] The phycobiliproteins themselves show little sequence evolution due to their highly constrained function (absorption and transfer of specific wavelengths). In some species of cyanobacteria, when both phycocyanin and phycoerythrin is present, the phycobilisome can undergo significant restructuring as response to light color. In green light the distal portions of the rods are made of red colored phycoerythrin, which absorbs green light better. In red light, this is replaced by blue colored phycocyanin, which absorbs red light better. This reversible process is known as complementary chromatic adaptation. It is the component of photosynthetic system of cyanobacteria, as a particle with which various structures are linked (i.e. thylakoid membrane, etc). ApplicationsPhycobilisomes can be used in [https://store-7fikt.mybigcommerce.com/product_images/uploaded_images/J_Fluorescence_PBXL_Detection.pdf prompt fluorescence],[3][4] flow cytometry,[5] Western blotting and protein microarrays. Some phycobilisomes have an absorption and emission profile similar to Cy5, they can be used in many of the same applications, however, they can be up to 200 times brighter, with a large Stokes shift, providing a larger signal per binding event. This property allows the detection of low-level target molecules]\\[5] or rare events. References1. ^Light Harvesting by Phycobilisomes Annual Review of Biophysics and Biophysical Chemistry Vol. 14: 47-77 (Volume publication date June 1985) 2. ^{{cite journal | vauthors = Lea-Smith DJ, Bombelli P, Dennis JS, Scott SA, Smith AG, Howe CJ | title = Phycobilisome-Deficient Strains of Synechocystis sp. PCC 6803 Have Reduced Size and Require Carbon-Limiting Conditions to Exhibit Enhanced Productivity | journal = Plant Physiology | volume = 165 | issue = 2 | pages = 705–714 | date = June 2014 | pmid = 24760817 | pmc = 4044857 | doi = 10.1104/pp.114.237206 | authorlink5 = Alison Gail Smith }} 3. ^{{cite journal | last1 = Zoha | first1 = Steven J. | last2 = Ramnarain | first2 = Shakuntala | last3 = Morseman | first3 = John P. | last4 = Moss | first4 = Mark W. | last5 = Allnutt | first5 = F. C. Thomas | last6 = Rogers | first6 = Yu-Hui | last7 = Harvey | first7 = Bronwen | name-list-format = vanc |title=PBXL Fluorescent Dyes for Ultrasensitive Direct Detection | journal = Journal of Fluorescence | date = 1999 | volume = 9 | issue = 3 | pages = 197–208 | doi = 10.1023/A:1022503600141 }} 4. ^{{cite web | title = MicroPlate Detection comparison between SureLight®P-3L, other fluorophores and enzymatic detection | url = https://store-7fikt.mybigcommerce.com/product_images/uploaded_images/Technical_Bulletin_3_ColBio_SureLightP3.pdf | publisher = Columbia Biosciences | date = 2010 }} 5. ^1 {{cite journal | vauthors = Telford WG, Moss MW, Morseman JP, Allnutt FC | title = Cyanobacterial stabilized phycobilisomes as fluorochromes for extracellular antigen detection by flow cytometry | journal = Journal of Immunological Methods | volume = 254 | issue = 1-2 | pages = 13–30 | date = August 2001 | pmid = 11406150 | url = https://store-7fikt.mybigcommerce.com/product_images/uploaded_images/Telford_Cyanobacterial_stabilized_phycobilisomes-2001.pdf }} External links
2 : Bacteriology|Photosynthesis |
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