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....
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Published in | IEEE journal of selected topics in quantum electronics Vol. 9; no. 2; pp. 177 - 188 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
New York
IEEE
01.03.2003
The Institute of Electrical and Electronics Engineers, Inc. (IEEE) |
Subjects | |
Online Access | Get full text |
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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. |
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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 |