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Amphidinium carterae

Hoffman, E., et al., 1996. Structural basis of light harvesting by carotenoids Peridinin-chlorophyll-protein from Amphidinium carterae. Science 272 1788-1791. [Pg.741]

Damjanovic, A., Ritz, T. and Schulten, K. (2000). Excitation transfer in the peridinin-chlorophyll-protein of Amphidinium carterae. Biophys. J. [Pg.69]

Results of investigations on the biosynthesis of neoxanthin (30) and peridinin (6) from 3H- and I4C-labeled mevanolate by the alga Amphidinium carterae are not in accordance with the formation of the exocyclic allene from an alkyne I. E. Swift, B. V. Milborrow, Biochem.J. 1981, 299, 69-74. [Pg.1037]

Eukaryotic plants and cyanobacteria. Photosynthetic dinoflagellates, which make up much of the marine plankton, use both carotenoids and chlorophyll in light-harvesting complexes. The carotenoid peridinin (Fig. 23-29), which absorbs blue-green in the 470- to 550-nm range, predominates. The LH complex of Amphidinium carterae consists of a 30.2-kDA protein that forms a cavity into which eight molecules of peridinin but only two of chlorophyll a (Chi a) and two molecules of a galactolipid are bound (Fig. 23-29).268... [Pg.1308]

Figure 23-29 (A) Stereoscopic drawing of light-harvesting complex from the dinoflagellate protozoan Amphidinium carterae. The central cavity contains eight molecules of peridinin, two of which can be seen protruding from the top. Deeply buried toward the bottom are two molecules of Chi a. Also present are two molecules of digalactosyl diacylglycerol. From Hofmann et al.268 Courtesy of Wolfram Welte. (B) Structure of peridinin. Figure 23-29 (A) Stereoscopic drawing of light-harvesting complex from the dinoflagellate protozoan Amphidinium carterae. The central cavity contains eight molecules of peridinin, two of which can be seen protruding from the top. Deeply buried toward the bottom are two molecules of Chi a. Also present are two molecules of digalactosyl diacylglycerol. From Hofmann et al.268 Courtesy of Wolfram Welte. (B) Structure of peridinin.
Increased synthesis of MAAs by exposure to high intensity artificial visible light also occurs in the Antarctic diatom Thalassiosira weissflogii, the prasinophyte Pyramimonas parkae, and most markedly in the dinoflagellate Amphidinium carterae (six-fold increase over control).171 However, high visible light exposure does not affect the MAA content of two other unicellular algae, Dunaliella tertiolecta (Chlorophyta) and Isochrysis sp. (Haptophyta). Supplemental exposures with UVA and UVB in combination and alone result in a variety of species-specific responses. [Pg.504]

Fig. 6 Cellular DMSP-to-carbon ratios (mol mol) versus specific growth rates under various nutrient limited conditions. Phaeocystis antarctica Fe limited (Stefels and van Leeuwe 1998) P. globosa P and N limited (Stefels unpublished carbon is calculated from cell volume see Table 1) Emiliania huxleyi, Amphidinium carterae and Thalassiosira pseudonana 1 N-limited chemostats (Keller et al. 1999b) T. pseudonana 2 Fe and CO2 limited (Sunda et al. 2002 carbon is calculated from cell volume see Table 1) T. pseudonana 3 N, P, Si and C02 limited (data are taken from the exponential and early stationary phase of growth, Figs. 2-7 in Bucciarelli and Sunda 2003 carbon is calculated from cell volumes, see Table 1)... Fig. 6 Cellular DMSP-to-carbon ratios (mol mol) versus specific growth rates under various nutrient limited conditions. Phaeocystis antarctica Fe limited (Stefels and van Leeuwe 1998) P. globosa P and N limited (Stefels unpublished carbon is calculated from cell volume see Table 1) Emiliania huxleyi, Amphidinium carterae and Thalassiosira pseudonana 1 N-limited chemostats (Keller et al. 1999b) T. pseudonana 2 Fe and CO2 limited (Sunda et al. 2002 carbon is calculated from cell volume see Table 1) T. pseudonana 3 N, P, Si and C02 limited (data are taken from the exponential and early stationary phase of growth, Figs. 2-7 in Bucciarelli and Sunda 2003 carbon is calculated from cell volumes, see Table 1)...
Franklin, D. J., and Berges, J. A. (2004). Mortality in cultures of the dinoflageUate Amphidinium carterae during culture senescence and darkness. Proc. R. Soc. Lond., B 271, 2099—2107. [Pg.1433]

Maitotoxin precursors are also produced by G. toxicus, Prorocentrum spp., Ostereopsis spp., Coolia monotis, Thecadinium sp., and Amphidinium carterae. [Pg.71]

FT Haxo, JH Kycia, GF Somers, A Bennett and HW Siegelman (1976) Peridinin-chlorophyll a protein of the dinoflegellate Amphidinium carterae (Plymouth 450). Plant Physiol 57 297-303. [Pg.249]

Amphidinium carterae also shows precisely where the carotenoid peridinin is located in this antenna complex (Hofmann et al., 1996 Fig. 11). Kiihlbrandt et al. (1994) have provided the atomic level structure of LHCllb, the major light harvesting Chi a/Chl b complex of plants and green algae this has allowed the rationalization of the proposed mechanisms of excitation energy transfer among the Chls. [Pg.15]

Fig. 2. Absorbance and circular dichroism spectra of sPCP from Amphidinium carterae. Mainform PCP represents the greater part of total sPCP, whereas HighSalt PCP is a minor form of high PI. a) native proteins b) isolated pigments in 80% acetone c) circular dichroism. The spectra have been normalized to the Chi a Qy absorbance at 670 nm or 663 nm respectively, or to the negative CD at 670 nm. (Sharpies et al., 1996)... Fig. 2. Absorbance and circular dichroism spectra of sPCP from Amphidinium carterae. Mainform PCP represents the greater part of total sPCP, whereas HighSalt PCP is a minor form of high PI. a) native proteins b) isolated pigments in 80% acetone c) circular dichroism. The spectra have been normalized to the Chi a Qy absorbance at 670 nm or 663 nm respectively, or to the negative CD at 670 nm. (Sharpies et al., 1996)...
Sharpies FP, Wrench PM and Hiller RG (1996) Two distinct forms of the peridinin-chlorophyll a-protein (PCP) from Amphidinium carterae. Biochim Biophys Acta 1276 117-123. [Pg.98]

Steck K, Wacker T, Welte W, Sharpies FP and Hiller RG (1990) Crystallization and preliminary X-ray analysis of a peridinin-chlorophyll a protein from Amphidinium carterae. FEES Lett 268 48-50... [Pg.98]

Echigoya, R. et al.. The structures of five new antifungal and hemolytic amphidinol analogs from Amphidinium carterae collected in New Zealand, Harmful Algae 4, 383, 2005. [Pg.751]

Carlucci and Bowes [29] showed that vitamin production in phytoplankton algae was attributed to release during exponential growth and upon cell death and lysis in old cultures. Vitamin utilization was readily observed in cultures of two species S. costatum produced utilizable biotin for Amphidinium carterae. The amount of utilizable vitamin and the rate at which it was exuded depended on the algal species and conditions of culturing. Aaronson et al. [149] showed that when O. danicus (chrysophyceae) was grown on a defined medium the cells excreted a number of vitamins including riboflavin, vitamin E and nicotinic acid in addition to four amino acids. Swift [150] published an excellent review of phytoplankton production, excretion and utihzation of vitamins. [Pg.139]

In the cell-free preparation of the Dinophyta Amphidinium carterae, " C-labellled zeaxanthin 14 was incorporated into neoxanthin 18, and then into acetylenic diadinoxanthin 67 and C37 peridinin 72 (Fig. 106.3). In addition, the three carbon atoms (C-13, 14, 20 ) of peridinin were eliminated from neoxanthin (C-13,14,20) [57, 58]. In organic chemistry, the C-7,8 double bond of zeaxanthin can be oxidized to the triple bond (acetylene group) of diatoxanthin 65 [59]. Enzymes for these reactions remain unknown. [Pg.3264]

Swift IE, Milborrow BV, Jeffrey SW (1982) Formatirai of neoxanthin, diadinoxanthin and peridinin from [ C]zeaxanthm by a cell-free system fiom Amphidinium carterae. Phytochemistry 21 2859-2864... [Pg.3279]

Fig. 1 (C) Structure of the complete peridinin-chlorophyll-protein trimer complex from the dinoflagellate Amphidinium carterae. The protein is depicted in ice blue, the carotenoids in red and the chlorophylls in green. Figure kindly produced by Robielyn Hagan from PDB file IPPR using VMD. Fig. 1 (C) Structure of the complete peridinin-chlorophyll-protein trimer complex from the dinoflagellate Amphidinium carterae. The protein is depicted in ice blue, the carotenoids in red and the chlorophylls in green. Figure kindly produced by Robielyn Hagan from PDB file IPPR using VMD.

See other pages where Amphidinium carterae is mentioned: [Pg.265]    [Pg.234]    [Pg.249]    [Pg.288]    [Pg.9]    [Pg.17]    [Pg.96]    [Pg.98]    [Pg.206]    [Pg.216]    [Pg.218]    [Pg.66]    [Pg.731]    [Pg.257]    [Pg.61]    [Pg.68]    [Pg.141]    [Pg.410]    [Pg.124]   
See also in sourсe #XX -- [ Pg.9 , Pg.15 , Pg.84 , Pg.206 ]

See also in sourсe #XX -- [ Pg.257 ]

See also in sourсe #XX -- [ Pg.141 ]




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