Journal ArticleDOI
The complete amino-acid sequence of the alpha and beta subunits of B-phycoerythrin from the rhodophytan alga Porphyridium cruentum.
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Determination of the complete amino-acid sequence of the subunits of B-phycoerythrin from Porphyridium cruentum has shown that the alpha subunit contains 164 amino- acid residues and the beta sub unit contains 177 residues.Abstract:
Determination of the complete amino-acid sequence of the subunits of B-phycoerythrin from Porphyridium cruentum has shown that the alpha subunit contains 164 amino-acid residues and the beta subunit contains 177 residues. When the sequences of B- and C-phycoerythrins are aligned with those of other phycobiliproteins, it is obvious that B-phycoerythrin lacks a deletion at beta-21-22 present in C-phycoerythrin. However, relative to C-phycoerythrin from Fremyella diplosiphon (Calothrix) (Sidler, W., Kumpf, B., Rudiger, W. and Zuber, H. (1986) Biol. Chem. Hoppe-Seyler 367, 627-642), B-phycoerythrin has deletions at beta-141k-o, beta-142, beta-143, beta-147 and beta-148. The four singly-linked phycoerythrobilins at positions alpha-84, alpha-143a, beta-84 and beta-155, and the doubly-linked phycoerythrobilin at position beta-50/61 are at sites homologous to the attachment sites in C-phycoerythrin. The aspartyl residues (alpha-87, beta-87, and beta-39), that interact with the bilins at alpha-84, beta-84, and beta-155 in C-phycocyanin, are found in the homologous positions in B-phycoerythrin. B-Phycoerythrin, in common with other phycobiliproteins, contains a N gamma-methylasparagine residue at position beta-72.read more
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Book ChapterDOI
Phycobilisome and Phycobiliprotein Structures
TL;DR: Phycobilisomes serve as the primary light-harvesting antennae for Photosystem II in cyanobacteria and red algae and contain smaller amounts ‘linker polypeptides,’ most of which do not bear chromophores.
Journal ArticleDOI
Recovery of pure B-phycoerythrin from the microalga Porphyridium cruentum.
TL;DR: B-phycoerythrin and R-phycocyanin in native state, from the red alga Porphyridium cruentum were obtained by an inexpensive and simple process using an anionic chromatographic column of DEAE cellulose.
Journal ArticleDOI
Evolution of the phycobiliproteins.
TL;DR: The phylogenetic analysis confirmed that the phycobiliprotein subfamilies, previously classified by their biochemical and spectroscopic properties, also formed coherent evolutionary groups, and supported a monophyletic separation of the eukaryotic sequences from the extant cyanobacterial sequences.
Book ChapterDOI
[14] Phycoerythrin fluorescence-based assay for reactive oxygen species
TL;DR: The assay for reactive oxygen species depends on the detection of chemical damage to phycoerythrin through the decrease in its fluorescence emission, and the effect of added compounds on the rate of this fluorescence loss is a measure of their ability to protect the protein.
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.
References
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Journal ArticleDOI
Light harvesting by phycobilisomes.
TL;DR: A CATALOGUE of PHYCOBILISOME COMPONENTS and a proposed nomenclature of Biliprotein Subunits.
Journal ArticleDOI
X-ray crystallographic structure of the light-harvesting biliprotein C-phycocyanin from the thermophilic cyanobacterium Mastigocladus laminosus and its resemblance to globin structures
TL;DR: The structure of the biliprotein C-phycocyanin from the thermophilic cyanobacterium Mastigocladus laminosus has been determined at 3 A resolution by X-ray diffraction methods and the electron density map could be improved by solvent flattening and has been interpreted in terms of the amino acid sequence.
Journal ArticleDOI
Refined three-dimensional structures of two cyanobacterial C-phycocyanins at 2.1 and 2.5 A resolution. A common principle of phycobilin-protein interaction.
TL;DR: The updated relative chromophore distances and orientations confirm the conclusion that hexameric aggregates are probably the basic functional units, and that inter-hexameric energy transfer takes place preferentially via the central B84 chromophores.
Book ChapterDOI
Structure and Function of Phycobilisomes: Light Harvesting Pigment Complexes in Red and Blue-Green Algae
TL;DR: This chapter focuses on the phycobilisome characteristics, their relationship to the photosystems in the thylakoid membrane, and major problems to be addressed in future investigations.
Journal ArticleDOI
Subunit structure and chromophore composition of rhodophytan phycoerythrins. Porphyridium cruentum B-phycoerythrin and b-phycoerythrin.
A N Glazer,C S Hixson +1 more
TL;DR: In this paper, a comparative study of the two phycoerythrins of the unicellular red alga Porphyridium cruentum is presented, and it is shown that the presence and amount of phycourobilin chromophores in the native protein is correlated with the presence of the gamma subunit.