Promising fluorescent probes from phycobiliproteins

Phycobiliproteins are brilliant-colored and water-soluble pigment-protein complexes existing widely in cyanobacteria, red algae, and cryptophytes. They function as predominant light-harvesting complexes to absorb the sunlight from 480 to 660 nm, and efficiently transfer the energy to chlorophyll a....

Full description

Saved in:
Bibliographic Details
Published inIEEE journal of selected topics in quantum electronics Vol. 9; no. 2; pp. 177 - 188
Main Authors Sun, Li, Wang, Shumei, Chen, Lixue, Gong, Xueqin
Format Journal Article
LanguageEnglish
Published New York IEEE 01.03.2003
The Institute of Electrical and Electronics Engineers, Inc. (IEEE)
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary:Phycobiliproteins are brilliant-colored and water-soluble pigment-protein complexes existing widely in cyanobacteria, red algae, and cryptophytes. They function as predominant light-harvesting complexes to absorb the sunlight from 480 to 660 nm, and efficiently transfer the energy to chlorophyll a. The phycobiliproteins are classified into three types based on their absorption spectra: phycoerythrin (PE), phycocyanin (PC), and allophycocyanin (AP). They are all composed of hetero-subunits /spl alpha/ and /spl beta/ and commonly exist in trimer (/spl alpha//spl beta/)3 or hexamer (/spl alpha//spl beta/)6 made up of equimolar monomer (/spl alpha//spl beta/). One monomer contains two to five chromophore phycobilins. In cyanobacteria and red algae, phycobiliproteins assemble a macromolecular particle, phycobilisome. Efficient excitation energy coupling among the chromophores in the phycobiliprotein trimer/hexamer and among the phycobiliproteins in the phycobilisome gives them some special spectroscopic properties superior to organic fluorescent dyes. These properties make the phycobiliproteins become promising fluorescent probes used in various fields of biological investigation.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ObjectType-Article-1
ObjectType-Feature-2
ISSN:1077-260X
1558-4542
DOI:10.1109/JSTQE.2003.812499