Effect of Light Quality on Phycobilisome Components of the Cyanobacterium Spirulina platensis. Babu, T. S., Kumar, A., & Varma, A. K. Plant Physiology, 95(2):492–497, February, 1991.
Effect of Light Quality on Phycobilisome Components of the Cyanobacterium Spirulina platensis [link]Paper  doi  abstract   bibtex   
Phycobilisomes from the nonchromatic adapting cyanobacterium Spirulina platensis are composed of a central core containing allophycocyanin and rods with phycocyanin and linker polypeptides in a regular array. Room temperature absorption spectra of phycobilisomes from this organism indicated the presence of phycocyanin and allophycocyanin. However, low temperature absorption spectra showed the association of a phycobiliviolin type of chromophore within phycobilisomes. This chromophore had an absorption maximum at 590 nanometers when phycobilisomes were suspended in 0.75 molar K-phosphate buffer (pH 7.0). Purified phycocyanin from this cyanobacterium was found to consist of three subparticles and the phycobiliviolin type of chromophore was associated with the lowest density subparticle. Circular dichroism spectra of phycocyanin subparticles also indicated the association of this chromophore with the lowest density subparticle. Absorption spectral analysis of α and β subunits of phycocyanin showed that phycobiliviolin type of chromophore was attached to the α subunit, but not the β subunit. Effect of light quality showed that green light enhanced the synthesis of this chromophore as analyzed from the room temperature absorption spectra of phycocyanin subparticles and subunits, while red or white light did not have any effect. Low temperature absorption spectra of phycobilisomes isolated from green, red, and white light conditions also indicated the enhancement of phycobiliviolin type of chromophore under green light.
@article{babu_effect_1991,
	title = {Effect of {Light} {Quality} on {Phycobilisome} {Components} of the {Cyanobacterium} {Spirulina} platensis},
	volume = {95},
	issn = {, 1532-2548},
	url = {http://www.plantphysiol.org/content/95/2/492},
	doi = {10.1104/pp.95.2.492},
	abstract = {Phycobilisomes from the nonchromatic adapting cyanobacterium Spirulina platensis are composed of a central core containing allophycocyanin and rods with phycocyanin and linker polypeptides in a regular array. Room temperature absorption spectra of phycobilisomes from this organism indicated the presence of phycocyanin and allophycocyanin. However, low temperature absorption spectra showed the association of a phycobiliviolin type of chromophore within phycobilisomes. This chromophore had an absorption maximum at 590 nanometers when phycobilisomes were suspended in 0.75 molar K-phosphate buffer (pH 7.0). Purified phycocyanin from this cyanobacterium was found to consist of three subparticles and the phycobiliviolin type of chromophore was associated with the lowest density subparticle. Circular dichroism spectra of phycocyanin subparticles also indicated the association of this chromophore with the lowest density subparticle. Absorption spectral analysis of α and β subunits of phycocyanin showed that phycobiliviolin type of chromophore was attached to the α subunit, but not the β subunit. Effect of light quality showed that green light enhanced the synthesis of this chromophore as analyzed from the room temperature absorption spectra of phycocyanin subparticles and subunits, while red or white light did not have any effect. Low temperature absorption spectra of phycobilisomes isolated from green, red, and white light conditions also indicated the enhancement of phycobiliviolin type of chromophore under green light.},
	language = {en},
	number = {2},
	urldate = {2015-12-01},
	journal = {Plant Physiology},
	author = {Babu, T. Sudhakar and Kumar, Ashok and Varma, Ajit K.},
	month = feb,
	year = {1991},
	pmid = {16668011},
	pages = {492--497},
}

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