ISSN:
1432-2056
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract R-phycoerythrin was purified from two benthic red algae, Iridaea cordata and Phyllophora antarctica, obtained growing at −2°C under thick sea ice off the coast of Antarctica. For the I. cordata protein, the molecular mass was 245,000 Da, and its secondary structure was 60% α helix, 17% β sheet, 16% turn, and 7% other. The light-harvesting faculties of the I. cordata protein resembled those of R-phycoerythrins from mesophilic red algae and were distinctive from the novel R-phycoerythrin from P. antarctica. Deconvolution of the visible absorption spectrum of R-phycoerythrin from I. cordata indicated a minimum of five component bands having maxima at 568, 558, 534, 496, and 481 nm. R-phycoerythrins from the mesophilic Porphyra tenera and psychrophilic Phyllophora antarctica had the same five bands. The protein from Phyllophora antarctica obtained its unique spectrum from a more intense component at 482 nm, and a less intense band at 533 nm. This change was probably produced by a replacement of phycoerythrobilin by phycourobilin. A temperature study of the circular dichroism CD was obtained for R-phycoerythrin from I. cordata from 4 to 80°C. Laser time-resolved fluorescence studies on R-phycoerythrin showed bilin to bilin energy transfer with a 60.2-ps lifetime, which should occur by the Förster resonance. The similarities in spectra between the proteins from I. cordata and Porphyra tenera and the different spectrum for the protein from Phyllophora antarctica show that only particular antarctic habitats require unique R-phycoerythrins.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/s003000050433
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