Primary structure of phycocyanin from the unicellular rhodophyte Cyanidium caldarium. II. Complete amino acid sequence of the beta subunit.

Troxler, Robert F.; Ehrhardt, Margaret M.; Brown-Mason, Anne; Offner, Gwynneth D.

doi:10.1016/s0021-9258(18)43250-4

Cited by 70 publications

(6 citation statements)

References 26 publications

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“…Phycobilisomes from C. caldarium contain allophycocyanin (plus linker proteins) in the core and phycocyanin as the only colored protein in the rods. The phycocyanin was purified as described earlier (Offner et al, 1981;Troxler et al, 1981) and concentrated to 15 mg/ml. The purity was measured by the ratio of absorbance at 620 nm (chromophore) and 280 nm (protein) and, in protein samples used for crystallization, was more than 8.…”

Section: Protein Purification and Crystallizationmentioning

confidence: 99%

Crystal Structure of C-Phycocyanin from Cyanidium caldarium Provides a New Perspective on Phycobilisome Assembly

Stec

Troxler

Teeter

1999

Biophysical Journal

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The crystal structure of the light-harvesting protein phycocyanin from the cyanobacterium Cyanidium caldarium with novel crystal packing has been solved at 1.65-A resolution. The structure has been refined to an R value of 18.3% with excellent backbone and side-chain stereochemical parameters. In crystals of phycocyanin used in this study, the hexamers are offset rather than aligned as in other phycocyanins that have been crystallized to date. Analysis of this crystal's unique packing leads to a proposal for phycobilisome assembly in vivo and for a more prominent role for chromophore beta-155. This new role assigned to chromophore beta-155 in phycocyanin sheds light on the numerical relationships among and function of external chromophores found in phycoerythrins and phycoerythrocyanins.

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Section: Protein Purification and Crystallizationmentioning

confidence: 99%

Crystal Structure of C-Phycocyanin from Cyanidium caldarium Provides a New Perspective on Phycobilisome Assembly

Stec

Troxler

Teeter

1999

Biophysical Journal

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“…The a subunit has one chromophore covalently attached to a cysteine, which is residue 84 from the N terminus, and the 0 subunit has two chromophores attached to cysteines at positions 84 and 155. [115][116][117] The X-ray crystallographic results for phycocyanin provide excellent data on the distances and orientations between the chromophores within a monomer, trimer, and hexamer.63-65 Since the rate of exciton transfer is extremely sensitive to distance (eq 14), careful analysis of each aggregation state and their varying of bilin-to-bilin distances is essential to understand the flow of excitons through the complex bilin matrix of a phycobilisome.…”

Section: F Exciton Migration In Phycocyanin Aggregatesmentioning

confidence: 99%

Phycocyanin in physical chemical studies

Berns¹,

MacColl²

1989

Chem. Rev.

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“…Protein analysis was conducted to evaluate what kind of phycobiliprotein was extracted with the respective extraction method and to detect protein modifications that might be characteristic for a specific extraction method, e.g., due to temperature effects. The presence of various types of phycobiliproteins in red algae and cyanobacteria is well described in the literature [ 44 , 45 , 46 ]. Indeed, allophycocyanin (APC), C-phycocyanin (C-PC) and R-phycocyanin (R-PC) were included in all samples.…”

Section: Discussionmentioning

confidence: 99%

Assessment of Phycocyanin Extraction from Cyanidium caldarium by Spark Discharges, Compared to Freeze-Thaw Cycles, Sonication, and Pulsed Electric Fields

et al. 2021

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Phycocyanin is a blue colored pigment, synthesized by several species of cyanobacteria and red algae. Besides the application as a food-colorant, the pigmented protein is of high interest as a pharmaceutically and nutritionally valuable compound. Since cyanobacteria-derived phycocyanin is thermolabile, red algae that are adapted to high temperatures are an interesting source for phycocyanin extraction. Still, the extraction of high quality phycocyanin from red algae is challenging due to the strong and rigid cell wall. Since standard techniques show low yields, alternative methods are needed. Recently, spark discharges have been shown to gently disintegrate microalgae and thereby enable the efficient extraction of susceptible proteins. In this study, the applicability of spark discharges for phycocyanin extraction from the red alga Cyanidium caldarium was investigated. The efficiency of 30 min spark discharges was compared with standard treatment protocols, such as three times repeated freeze-thaw cycles, sonication, and pulsed electric fields. Input energy for all physical methods were kept constant at 11,880 J to ensure comparability. The obtained extracts were evaluated by photometric and fluorescent spectroscopy. Highest extraction yields were achieved with sonication (53 mg/g dry weight (dw)) and disintegration by spark discharges (4 mg/g dw) while neither freeze-thawing nor pulsed electric field disintegration proved effective. The protein analysis via LC-MS of the former two extracts revealed a comparable composition of phycobiliproteins. Despite the lower total concentration of phycocyanin after application of spark discharges, the purity in the raw extract was higher in comparison to the extract attained by sonication.

show abstract

Primary structure of phycocyanin from the unicellular rhodophyte Cyanidium caldarium. II. Complete amino acid sequence of the beta subunit.

Cited by 70 publications

References 26 publications

Crystal Structure of C-Phycocyanin from Cyanidium caldarium Provides a New Perspective on Phycobilisome Assembly

Crystal Structure of C-Phycocyanin from Cyanidium caldarium Provides a New Perspective on Phycobilisome Assembly

Phycocyanin in physical chemical studies

Assessment of Phycocyanin Extraction from Cyanidium caldarium by Spark Discharges, Compared to Freeze-Thaw Cycles, Sonication, and Pulsed Electric Fields

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