Journal ArticleDOI
Cryptomonad biliproteins: Bilin types and locations.
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TLDR
There is no conserved location for the bilin with longest wavelength visible absorption band among these proteins, and, consequently, that there is no Conserved energy transfer pathway common to all native cryptophycean biliproteins.Abstract:
Two crytophycean phycocyanins (Cr-PCs), Hemiselmis strain HP9001 Cr-PC 612 and Falcomonas daucoides Cr-PC 69 were purified and characterized with respect to bilin numbers, types and locations. Each biliprotein carried one bilin on the α subunit and three on the β subunit. Cr-PC 612 carried phycocyanobilin at α-Cys-18, β-Cys-82, and β-Cys-158, and a doubly-linked 15,16-dihydrobiliverdin at β-DiCys-50,61. Cr-PC 569 carried phycocyanobilin at α-Cys-18 and β-Cys-82, a singly-linked Bilin 584 at β-Cys-158, and a doubly-linked Bilin 584 at β-DiCys-50,61. This work, in conjunction with earlier studies on Cr-PE 545, Cr-PE 555, Cr-PE 566, and Cr-PC 645, shows that there is no conserved location for the bilin with longest wavelength visible absorption band among these proteins, and, consequently, that there is no conserved energy transfer pathway common to all native cryptophycean biliproteins. Only phycocyanobilin or phycoerythrobilin is found at β-Cys-82; there is greater bilin variability at the other three attachment sites.read more
Citations
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Functional Genomic Analysis of the HY2 Family of Ferredoxin-Dependent Bilin Reductases from Oxygenic Photosynthetic Organisms
TL;DR: Three new classes of bilin reductases with distinct substrate/product specificities that are involved in the biosynthesis of the phycobiliprotein chromophore precursors phycoerythrobilin andphycocyanobilin are defined.
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Electronic coherence lineshapes reveal hidden excitonic correlations in photosynthetic light harvesting
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TL;DR: Two-dimensional electronic spectroscopy is used to examine energy transfer at ambient temperature in a naturally occurring light-harvesting protein and provides a probe of the adiabaticity of the free energy landscape underlying light harvesting.
References
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Phycobilisome a macromolecular complex optimized for light energy transfer
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Chromophore Content of Blue-Green Algal Phycobiliproteins
Alexander N. Glazer,Suen Fang +1 more
TL;DR: The chromophore content of blue-green algal phycocyanin and allophycocianin, derived from a unicellular blue- green alga of Synechococcus sp.
Journal ArticleDOI
Isolation, crystallization, crystal structure analysis and refinement of B-phycoerythrin from the red alga Porphyridium sordidum at 2.2 A resolution.
TL;DR: The light-harvesting pigment-protein complex B-phycoerythrin from the red alga Porphyridium sordidum has been isolated and crystallized and has been refined by energy-restrained crystallographic refinement and model building.
Journal ArticleDOI
Phycoerythrins of marine unicellular cyanobacteria. I. Bilin types and locations and energy transfer pathways in Synechococcus spp. phycoerythrins.
L.J. Ong,Alexander N. Glazer +1 more
TL;DR: The adaptations to blue-green light, high PUB content and the presence of an additional bilin on the alpha subunit, increase the efficiency of light absorption by PE(II)s at approximately 500 nm.