Phycobilin
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Phycobilins are photosynthetic pigments found in cyanobacteria and in the chloroplasts of red algae, glaucophytes and some cryptomonads (though not in green algae and higher plants). They are unique among the photosynthetic pigments in that they are bonded to certain water-soluble proteins, known as phycobiliproteins; phycobilins serve as chromophores (the light-capturing part) of the phycobiliproteins. Phycobiliproteins capture light energy which is then passed on to chlorophylls during photosynthesis.
The phycobilins are especially efficient at absorbing red, orange, yellow and green light, wavelengths which are not well absorbed by chlorophyll a. Organisms growing in shallow waters tend to contain phycobilins that can capture yellow/red light, while those at greater depth often contain more of the phycobilins that can capture green light, which is more abundant there.
There are several types of phycobilins: phycourobilin, phycoerythrobilin, cryptoviolin and phycocyanobilin. They can be found in different combinations attached to phycobiliproteins to confer specific spectroscopic properties.
Chemically, phycobilins consist of an open chain of four pyrrole rings (tetrapyrrole) and are structurally similar to the bile pigment bilirubin. (Bilirubin's structure is also affected by light, a fact used for the phototherapy of jaundiced newborns.) Phycobilins are also closely related to the chromophores of the light-detecting plant pigment phytochrome which also consist of an open chain of four pyrroles. Chlorophylls are composed of four pyrroles as well, but there they are arranged in a ring and contain a metal atom in the center.
The phycobilins fluoresce at a particular wavelength, and are therefore often used in research as chemical tags, e.g. by binding phycobiliproteins to antibodies in a technique known as immunofluorescence.
The name phycobilin comes from the Greek phyco- for "algae", and bilin referring to bile.
Reference
- O'Carra P, Murphy RF, Killilea SD. "The native forms of the phycobilin chromophores of algal biliproteins. A clarification." Biochem J. 1980 May 1;187(2):303-9. PMID 7396851