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((Refimprove|date=December 2009))
'''Phycobiliproteins''' are water-soluble [[protein]]s present in [[cyanobacteria]] and certain algae ([[rhodophyte]]s, [[cryptomonad]]s, [[glaucocystophytes]]). They capture light energy, which is then passed on to [[chlorophyll]]s during [[photosynthesis]]. Phycobiliproteins are formed of a complex between proteins and  [[covalent]]ly bound [[phycobilin]]s that act as [[chromophore]]s (the light-capturing part).  They are most important constituents of the [[phycobilisome]]s.
[[File:Phycobilisome structure.jpg|thumb|Phycobilisome structure]]
==Major phycobiliproteins==
{| class="wikitable" border="1"
|-
! '''Phycobiliprotein'''
! MW ([[atomic mass unit|kDa]])
! Ex (nm) / Em (nm)
! [[Quantum yield]]
! Molar [[Mass attenuation coefficient|Extinction Coefficient]] (M<sup>−1</sup>cm<sup>−1</sup>)
! Comment
! Image
|-
| '''R-[[Phycoerythrin]] (R-PE)'''
| 240
| 498.546.566&nbsp;nm / 576&nbsp;nm
| 0,84
| 1.53 10<sup>6</sup>
| Can be excited by Kr/Ar laser<br/>'''Applications for R-Phycoerythrin'''

Many applications and instruments were developed specifically for R-phycoerythrin.  It is commonly used in immunoassays such as FACS, flow cytometry, multimer/tetramer applications.

'''Structural Characteristics'''

R-phycoerythrin is also produced by certain red algae.  The protein is made up of at least three different subunits and varies according to the species of algae that produces it. The subunit structure of the most common R-PE is (αβ)<sub>6</sub>γ. The α subunit has two phycoerythrobilins (PEB), the β subunit has 2 or 3 PEBs and one phycourobilin (PUB), while the different gamma subunits are reported to have 3 PEB and 2 PUB (γ<sub>1</sub>) or  1 or 2 PEB and 1 PUB (γ<sub>2</sub>).

[http://www.columbiabiosciences.com/phycobiliproteins-1/ (Phycobiliprotein overview information)]
|[[File:R-phycoerythrin 1EYX 1 of 2.gif|thumb|none|250px|The crystal structure of R-phycoerythrin from [[red algae]] ''[[Gracilaria|Gracilaria chilensis]]'' ([[Protein Data Bank|PDB]] ID: 1EYX <ref name=PDB1EYX>((Cite journal |url=http://www.rcsb.org/pdb/explore/explore.do?structureId=1EYX |title=Crystal structure of R-phycoerythrin at 2.2 angstroms |author=Contreras-Martel, C. |display-authors=4 |author2=Legrand, P. |author3=Piras, C. |author4=Vernede, X. |author5=Martinez-Oyanedel, J. |author6=Bunster, M. |author7=Fontecilla-Camps, J.C. |date=2000-05-09 |publisher=RCSB Protein Data Bank (PDB) |id=PDB ID: 1EYX |doi=10.2210/pdb1eyx/pdb |access-date=11 October 2012))</ref><ref name=ContrerasMartel01>((cite journal | vauthors = Contreras-Martel C, Martinez-Oyanedel J, Bunster M, Legrand P, Piras C, Vernede X, Fontecilla-Camps JC | title = Crystallization and 2.2 A resolution structure of R-phycoerythrin from Gracilaria chilensis: a case of perfect hemihedral twinning | journal = Acta Crystallographica D | volume = 57 | issue = Pt 1 | pages = 52–60 | date = January 2001 | pmid = 11134927 | doi = 10.1107/S0907444900015274 | s2cid = 216930 | id = PDB ID: 1EYX | doi-access =  ))</ref><ref name="RasTop">Image created with [http://www.geneinfinity.org/rastop/ RasTop] (Molecular Visualization Software).</ref>) - basic [[oligomer]] (((color|green|α))((color|blue|β))((color|red|γ)))<sub>2</sub> (so called asymmetric unit). It contains ((color|#BF00BF|phycocyanobilin)), ((color|#FF40FF|biliverdine IX alpha)), ((color|#FF80FF|phycourobilin)), ((color|#FF6600|N-methyl asparagine)), ((color|#FFD500|SO<sub>4</sub><sup>2−</sup>)). One fragment of γ chain is red, second one white because it is not considered as [[alpha helix]] despite identical aminoacid sequence.]]
|-
| '''B-[[Phycoerythrin]] (B-PE)'''
| 240
| 546.566&nbsp;nm / 576&nbsp;nm
| 0,98
| (545&nbsp;nm) 2.4 10<sup>6</sup>
(563&nbsp;nm) 2.33 10<sup>6</sup>
|'''Applications for B-Phycoerythrin'''

Because of its high quantum yield, B-PE is considered the world's brightest fluorophore.   It is compatible with commonly available lasers and gives exceptional results in flow cytometry, Luminex and immunofluorescent staining.  B-PE is also less "sticky" than common synthetic fluorophores and therefore gives less background interference.

''' Structural Characteristics'''

B-phycoerythrin (B-PE) is produced by certain red algae such as ''Rhodella'' sp.  The specific spectral characteristics are a result of the composition of its subunits. B-PE is composed of at least three subunits and sometimes more.  The chromophore distribution is as follows:   α subunit  with 2 phycoerythrobilins (PEB), β subunit with 3 PEB, and the γ subunit with 2 PEB and 2 phycourobilins (PUB).  The quaternary  structure is reported as (αβ)<sub>6</sub>γ.

[http://www.columbiabiosciences.com/phycobiliproteins-1/ (Phycobiliprotein overview information)]
|[[File:B-phycoerythrin 3V57.png|thumb|none|250px|The crystal structure of B-phycoerythrin from [[red algae]] ''[[Porphyridium cruentum]]'' ([[Protein Data Bank|PDB]] ID: 3V57 <ref name=PDB3V57>((Cite journal |url=http://www.rcsb.org/pdb/explore/explore.do?structureId=3V57 |title=Crystal Structure of the B-phycoerythrin from the red algae ''Porphyridium cruentum'' at pH8 |author=Camara-Artigas, A. |date=2011-12-16 |publisher=RCSB Protein Data Bank (PDB) |id=PDB ID: 3V57 |doi=10.2210/pdb3v57/pdb |access-date=12 October 2012))</ref><ref name=CamaraArtigas12>((cite journal | vauthors = Camara-Artigas A, Bacarizo J, Andujar-Sanchez M, Ortiz-Salmeron E, Mesa-Valle C, Cuadri C, Martin-Garcia JM, Martinez-Rodriguez S, Mazzuca-Sobczuk T, Ibañez MJ, Allen JP | title = pH-dependent structural conformations of B-phycoerythrin from Porphyridium cruentum | journal = The FEBS Journal | volume = 279 | issue = 19 | pages = 3680–3691 | date = October 2012 | pmid = 22863205 | doi = 10.1111/j.1742-4658.2012.08730.x | s2cid = 31253970 | id = PDB ID: 3V57 ))</ref><ref name="RasTop" />). The asymmetric unit (((color|green|α))((color|blue|β)))<sub>2</sub> on the left and assumed biological molecule (((color|green|α))((color|blue|β)))<sub>3</sub>. It contains ((color|#FF40FF|phycoerythrobilin)), ((color|#FF6600|N-methyl asparagine)) and ((color|#FFD500|SO<sub>4</sub><sup>2−</sup>)).]]
|- 
| '''C-[[Phycocyanin]] (CPC)'''
| 232
| 620&nbsp;nm / 642&nbsp;nm
| 0,81
| 1.54 10<sup>6</sup>
| Accepts the fluorescence for R-PE; Its red fluorescence can be transmitted to Allophycocyanin
|
|-
| '''[[Allophycocyanin]] (APC)'''
| 105
| 651&nbsp;nm / 662&nbsp;nm
| 0,68
| 7.3 10<sup>5</sup>
| Excited by He/Ne laser; double labeling with Sulfo-Rhodamine 101 or any other equivalent fluorochrome.<br/>'''Applications for Allophycocyanin'''

Many applications and instruments were developed specifically for allophycocyanin. It is commonly used in immunoassays such as flow cytometry and high-throughput screening. It is also a common acceptor dye for FRET assays.

'''Structural Characteristics '''

Allophycocyanin can be isolated from various species of red or blue-green algae, each producing slightly different forms of the molecule. It is composed of two different subunits (α and β) in which each subunit has one phycocyanobilin (PCB) chromophore. The subunit structure for APC has been determined as (αβ)<sub>3</sub>.

[http://www.columbiabiosciences.com/phycobiliproteins-1/ (Phycobiliprotein overview information)]
| [[File:2vjt.jpg|thumb|250px|Allophycocyanin dodekamer + 12 phycocyanobilin (green), ''[[Gloeobacter violaceus]]'']]
|-
| colspan=6 rowspan=1 | ↑ = [[FluoProbes]] [http://www.interchim.fr/ft/2/28310A.pdf PhycoBiliProteins data]
|-
|}

== Characteristics ==
Phycobiliproteins demonstrate superior fluorescent properties compared to small organic fluorophores, especially when high sensitivity or multicolor detection required :
* Broad and high absorption of light suits many light sources
* Very intense emission of light: 10-20 times brighter than small organic fluorophores
* Relative large [[Stokes shift]] gives low background, and allows multicolor detections.
* Excitation and emission spectra do not overlap compared to conventional organic dyes.
* Can be used in tandem (simultaneous use by [[Förster resonance energy transfer|FRET]]) with conventional chromophores (i.e. PE and FITC, or APC and SR101 with the same light source).
* Longer fluorescence retention period.
* High water solubility

== Applications ==
Phycobiliproteins allow very high detection sensitivity, and can be used in various fluorescence based techniques [https://store-7fikt.mybigcommerce.com/product_images/uploaded_images/Telford_Cyanobacterial_stabilized_phycobilisomes-2001.pdf fluorimetric microplate assays] ((Webarchive|url=https://web.archive.org/web/20180318182543/https://store-7fikt.mybigcommerce.com/product_images/uploaded_images/Telford_Cyanobacterial_stabilized_phycobilisomes-2001.pdf |date=2018-03-18 )),<ref>((Cite journal|title=MicroPlate Detection comparison between SureLight P-3L, other fluorophores and enzymatic detection Table 1: Comparison of honeypot with other detection methods.|journal=Columbia Biosciences|year=2010|doi=10.7717/peerj-cs.350/table-1 |doi-access=free))</ref><ref>((cite web |url=https://store-7fikt.mybigcommerce.com/product_images/uploaded_images/Telford_Cyanobacterial_stabilized_phycobilisomes-2001.pdf |title=Flow Cytometry |access-date=2014-06-07 |archive-date=2018-03-18 |archive-url=https://web.archive.org/web/20180318182543/https://store-7fikt.mybigcommerce.com/product_images/uploaded_images/Telford_Cyanobacterial_stabilized_phycobilisomes-2001.pdf |url-status=dead ))</ref><ref>((Cite journal|last1=Telford|first1=William G|last2=Moss|first2=Mark W|last3=Morseman|first3=John P|last4=Allnutt|first4=F.C.Thomas|date=August 2001|title=Cyanobacterial stabilized phycobilisomes as fluorochromes for extracellular antigen detection by flow cytometry|url=http://dx.doi.org/10.1016/s0022-1759(01)00367-2|journal=Journal of Immunological Methods|volume=254|issue=1–2|pages=13–30|doi=10.1016/s0022-1759(01)00367-2|pmid=11406150 |issn=0022-1759))</ref> FISH and multicolor detection.

They are under development for use in [[artificial photosynthesis]], limited by the relatively low conversion efficiency of 4-5%.<ref>((Cite web|last=Lavars|first=Nick|date=2021-10-19|title=Encasing algae triples the efficiency of artificial photosynthesis|url=https://newatlas.com/energy/algae-artificial-photosynthesis-efficiency-liquid-crystal-ntu/|access-date=2021-10-24|website=New Atlas|language=en-US))</ref>

==References==
<references/>

((Protein topics))

[[Category:Photosynthetic pigments]]
[[Category:Cyanobacteria proteins]]
[[Category:Algae]]
[[Category:Bacterial proteins]]

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