Phycoerythrins of several species of the higher red alga Callithamnion show virtually identical spectra, typical of R-phycoerythrins, with absorption maxima at 565, 539, and 497 nanometers. One species, Callithamnion roseum, produces a phycoerythrin lacking the peak at 539 nanometers. Comparison of a "typical" R-phycoerythrin from Callithamnion byssoides with the "atypical" phycoerythrin of C. roseum shows that both proteins carry 35 bilins per native molecule of 240,000 daltons; however, C. byssoides phycoerythrin carries 27.6 phycoerythrobilin and 7.3 phycourobilin groups, whereas C. roseum phycoerythrin carries 24.1 phycoerythrobilin and 10.9 phycourobilin groups. These differences in the relative amounts of the bilin prosthetic groups account in large measure for the differences between the absorption spectra of the native proteins. The ratio of phycoerythrobilin to phycourobilin in C. roseum phycoerythrin can be modulated by varying the light intensity during growth.Data on the physical, immunological and spectroscopic properties of Callithamnion phycoerythrins indicate that the variation in the relative number of the two bilin prosthetic groups does not affect significantly the conformation of the biliprotein.
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http://dx.doi.org/10.1104/pp.68.2.482 | DOI Listing |
Food Res Int
August 2024
Department of Food Science, Aarhus University, Agro Food Park 48, 8200 Aarhus N, Denmark; CBIO, Aarhus University Centre for Circular Bioeconomy, 8830 Tjele, Denmark; CiFOOD, Aarhus University Centre for Innovative Food Research, 8000 Aarhus C, Denmark. Electronic address:
R-phycoerythrin (R-PE) is the most abundant, naturally occurring phycobiliproteins found in red algae. The spectroscopic and structural properties of phycobiliproteins exhibit unique absorption characteristics with two significant absorption maxima at 498 and 565 nm, indicating two different chromophores of R-PE, phycourobilin and phycoerythrobilin respectively. This study aimed to clarify how the stability of R-PE purified from F.
View Article and Find Full Text PDFFront Microbiol
February 2024
Sorbonne Université, CNRS, UMR 7144 Adaptation and Diversity in the Marine Environment (AD2M), Station Biologique de Roscoff (SBR), Roscoff, France.
, the second most abundant marine phytoplanktonic organism, displays the widest variety of pigment content of all marine oxyphototrophs, explaining its ability to colonize all spectral niches occurring in the upper lit layer of oceans. Seven pigment types (PTs) have been described so far based on the phycobiliprotein composition and chromophorylation of their light-harvesting complexes, called phycobilisomes. The most elaborate and abundant PT (3d) in the open ocean consists of cells capable of type IV chromatic acclimation (CA4), i.
View Article and Find Full Text PDFPlant J
May 2024
National Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan, 430070, P.R. China.
CpcL-phycobilisomes (CpcL-PBSs) are a reduced type of phycobilisome (PBS) found in several cyanobacteria. They lack the traditional PBS terminal energy emitters, but still show the characteristic red-shifted fluorescence at ~670 nm. We established a method of assembling in vitro a rod-membrane linker protein, CpcL, with phycocyanin, generating complexes with the red-shifted spectral features of CpcL-PBSs.
View Article and Find Full Text PDFChembiochem
October 2023
Department of Chemistry, University of Houston, 3585 Cullen Blvd, Houston, TX, 77204, USA.
Cyanobacteriochrome (CBCR) cGMP-specific phosphodiesterase, adenylyl cyclase, and FhlA (GAF) domains bind bilin cofactors to confer sensory wavelengths important for various cyanobacterial photosensory processes. Many isolated GAF domains autocatalytically bind bilins, including the third GAF domain of CBCR Slr1393 from Synechocystis sp. PCC6803, which binds phycoerythrobilin (PEB) to yield a bright orange fluorescent protein.
View Article and Find Full Text PDFbioRxiv
May 2023
Department of Chemistry, University of Houston, 3585 Cullen Blvd, Houston, TX, 77204 (USA).
Cyanobacteriochrome (CBCR) GAF domains bind bilin cofactors to confer sensory wavelengths important for various cyanobacterial photosensory processes. Many isolated GAF domains autocatalytically bind bilins, becoming fluorescent. The third GAF domain of CBCR Slr1393 from sp.
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