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  • 1
    Electronic Resource
    Electronic Resource
    Distribution of the chlorophyll spectral forms in the chlorophyll-protein complexes of photosystem II antenna (1993)
    s.l. : American Chemical Society
    Biochemistry 32 (1993), S. 3203-3210 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00064a002
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  • 2
    Electronic Resource
    Electronic Resource
    Gaussian Decomposition of Absorption and Linear Dichroism Spectra of Outer Antenna Complexes of Photosystem II (1994)
    s.l. : American Chemical Society
    Biochemistry 33 (1994), S. 8982-8990 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00196a016
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  • 3
    Electronic Resource
    Electronic Resource
    Ionic permeability of the mitochondrial outer membrane (1992)
    Springer
    European biophysics journal 20 (1992), S. 311-319 
    Details
    ISSN: 1432-1017
    Keywords: Mitochondria ; Ionic channels ; Mitochondrial outer membrane ; Patch clamp
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract The ionic permeability of the outer mitochondrial membrane (OMM) was studied with the patch clamp technique. Electrical recording of intact mitochondria (hence of the outer membrane (OM)), derived from mouse liver, showed the presence of currents corresponding to low conductances (〈 50 pS), as well as of four distinct conductances of 99 pS,152 pS, 220 pS and 307 pS (in 150 mM KCl). The latter were voltage gated, being open preferentially at positive (pipette) potentials. Very similar currents were found by patch clamping liposomes containing the isolated OM derived from rat brain mitochondria. Here a conductance of approximately 530 pS, resembling in its electrical characteristics a conductance already attributed to mitochondrial contact sites (Moran et al. 1990), was also detected. Immunoblot assays of mitochondria and of the isolated OM with antibodies against the outer membrane voltage-dependent anion channel (VDAC) (Colombini 1979), showed the presence of the anion channel in each case. However, the typical electrical behaviour displayed by such a channel in planar bilayers could not be detected under our experimental conditions. From this study, the permeability of the OMM appears different from what has been reported hitherto, yet is more in line with that multifarious and dynamic structure which apparently should belong to it, at least within the framework of mitochondrial biogenesis (Pfanner and Neupert 1990).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00196590
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  • 4
    Electronic Resource
    Electronic Resource
    Novel aspects of chlorophyll a/b-binding proteins (1997)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 100 (1997), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The light-harvesting proteins (LHC) constitute a multigene family including, in higher plants, at least 12 members whose location, within the photosynthetic membrane, relative abundance and putative function appear to be very different. The major light-harvesting complex of photosystem II (LHCII) is the most abundant membrane protein in the biosphere and fulfil a constitutive light-harvesting function for photosystem II while the early light-induced proteins (ELIPs) are expressed in low amounts under stress conditions. Primary sequence analysis suggests that all these proteins share a common structure which was resolved at 3.7 Å resolution by electron crystallography in the case of the major LHCII complex: Three transmembrane helices connected by hydrophilic loops coordinate seven chlorophyll a and five chlorophyll b molecules by histidine, glutamine, asparagine lateral chains as well as by charge compensated ionic pairs of glutamic acid and arginine residues; moreover, at least two xantophyll molecules are located at the centre of the structure in close contact with seven porphyrins, tentatively identified as chlorophyll a. The antenna system is also involved in the regulation of excitation energy transfer to reaction centre II. This function has been attributed to three members of the protein family, namely CP29, CP26 and CP24 (also called minor chlorophyll proteins) which have been recently characterised and shown to bind most of the xantophyll cycle carotenoids, thus suggesting that the non-photochemical quenching mechanism is acting in these proteins. Further support to this assignment comes from the recent identification of protonation sites in CP29 and CP26 by covalent dicyclohexhylcarbodiimide binding suggesting that these respond to low lumenal pH. In addition, CP29 is reversibly phosphorylated under light and cold stress conditions, undergoing conformational change, supporting the hypothesis that these subunits, present in low amounts in photosystem II, have a major regulatory role in the light-harvesting function and are thus important in environmental stress resistance.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1997.tb00004.x
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  • 5
    Electronic Resource
    Electronic Resource
    Mechanistic aspects of the xanthophyll dynamics in higher plant thylakoids (2003)
    Oxford, UK : Munksgaard International Publishers
    Physiologia plantarum 119 (2003), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Plant thylakoids have a highly conserved xanthophyll composition, consisting of β-carotene, lutein, neoxanthin and a pool of violaxanthin that can be converted to antheraxanthin and zeaxanthin in excess light conditions. Recent work has shown that xanthophylls undergo dynamic changes, not only in their composition but also in their distribution among Lhc proteins. Xanthophylls are released from specific binding site in the major trimeric LHCII complex of photosystem II and are subsequently bound to different sites into monomeric Lhcb proteins and dimeric Lhca proteins. In this work we review available evidence from in vivo and in vitro studies on the structural determinants that control xanthophyll exchange in Lhc proteins. We conclude that the xanthophyll exchange rate is determined by the structure of individual Lhc gene products and it is specifically controlled by the lumenal pH independently from the activation state of the violaxanthin de-epoxidase enzyme. The xanthophyll exchange induces important modifications in the organization of the antenna system of Photosystem II and, possibly of Photosystem I. Major changes consist into a modulation of the light harvesting efficiency and an increase of the protection from lipid peroxidation. The xanthophyll cycle thus appears to be a signal transduction system for co-ordinated regulation of the photoprotection mechanisms under persistent stress from excess light.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1399-3054.2003.00213.x
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  • 6
    Electronic Resource
    Electronic Resource
    Immunological studies on chlorophyll-a/b proteins and their distribution in thylakoid membrane domains (1990)
    Springer
    Planta 181 (1990), S. 275-286 
    Details
    ISSN: 1432-2048
    Keywords: Chloroplast membranes, proteins (lateral heterogeneity, state I-state II transition) ; Light-harvesting complexes ; State I-State II transition ; Thylakoid proteins ; Zea (chloroplast proteins)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The immunological relationships between chlorophyll-a/b proteins from higher-plant thylakoid membranes have been studied by assaying purified chlorophyll proteins (CPs) with polyclonal and monoclonal antibodies. Although low levels of cross-reactions were observed between all light-harvesting proteins, the peripheral antennae (LHCII) were largely distinct from the inner antennae (CP 26 and CP 29). Chlorophyll-protein 24 and LHCI-680 have been proposed to have a role in connecting the inner and outer antennae, respectively, in photosystems I and II, and were closely related. The immunological relationships closely corresponded to the spectral properties. Antibodies were also used for locating chlorophyll-a/b proteins in grana, stroma and bundle-sheath membranes showing a strong lateral heterogeneity, which was maintained following State I State II transition. The only exception to this pattern was a specific LHCII population enriched in State-II stroma membranes. Chlorophyll proteins from bundlesheath chloroplasts, that have only cyclic electron flow, had epitopes distinct from those of their mesophyll homologues.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00195877
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  • 7
    Electronic Resource
    Electronic Resource
    Identification and characterization of photosystem II chlorophyll a/b binding proteins in Marchantia polymorpha L. (1998)
    Springer
    Planta 204 (1998), S. 260-267 
    Details
    ISSN: 1432-2048
    Keywords: Key words: Marchantia (liverwort) ; Minor chlorophyll a/b-binding proteins (CP24 ; CP26 ; CP29) ; Photosystem II antenna organization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. The minor chlorophyll a/b-binding (CAB) proteins of the liverwort Marchantia polymorpha L. were investigated in order to compare the antenna organization and the light-acclimation potential in lower and higher plants. Homologues to the minor CAB proteins CP24, CP26 and CP29 were identified by the following criteria: enrichment in photosystem II preparations, immunological cross-reactivities, spectroscopic properties and protein-fragment amino acid sequences. The high violaxanthin content of the minor CAB proteins in M. polymorpha indicates that their role in protection from high light is comparable in lower and higher plants. Considerably more-alkaline isoelectric points are found for the minor CAB proteins of M. polymorpha than for their higher-plant counterparts. This might be due to a higher content of basic amino acids. While the N-terminal sequence of angiosperm CP29 contains a threonine that becomes phosphorylated during cold stress, this amino acid is substituted by valine in M. polymorpha. Therefore, the regulatory properties of this protein could differ in lower and higher plants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004250050255
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  • 8
    Electronic Resource
    Electronic Resource
    The chlorophyll-a/b proteins of photosystem II in Chlamydomonas reinhardtii (1991)
    Springer
    Planta 183 (1991), S. 423-433 
    Details
    ISSN: 1432-2048
    Keywords: Chlamydomonas (light-harvesting complexes) ; Chlorophyll a/b protein (chlamydomonas) ; Light-harvesting complex
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have adapted the procedure for the isolation of PSII membranes from higher plants (D.A. Berthold et al., 1981, FEBS Lett. 134, 231–234) to the green algae Chlamydomonas reinhardtii. The chlorophyll (Chl)-binding proteins from this PSII preparation have been further separated into single Chl-binding polypeptides and characterized spectroscopically. Seven single polypeptides were shown to bind Chl a and Chl b. In particular, we demonstrate that polypeptides p9, p10 and p22, which had not been previously shown to bind Chl a and b, have characteristics similar to those of CP29, CP26 and CP24 from higher plants. We note, however, that p9 and p10 are phosphorylatable in C. reinhardtii, at variance with CP29 and CP26 from higher plants. Our data support the notion that the PSII antenna systems in C. reinhardtii and in higher plants are very similar. Therefore, studies on the organization and regulation of light-harvesting processes in C. reinhardtii may provide information of general relevance for both green algae and higher plants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00197742
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  • 9
    Electronic Resource
    Electronic Resource
    Chlorophyll-proteins from maize seedlings grown under intermittent light conditions (1993)
    Springer
    Planta 191 (1993), S. 265-273 
    Details
    ISSN: 1432-2048
    Keywords: Chlorophyll-protein complex (stoichiometry) ; Chloroplast development ; Intermittent light ; Photosynthetic pigment ; Photosystem II ; Zea
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We studied the organization of the antenna system of maize (Zea mays L.) seedlings grown under intermittent light conditions for 11 d. These plants had a higher chlorophyll-a/b ratio, a higher ratio of carotenoids to chlorophyll and a lower ratio of chlorophyll to protein than plants grown in continuous light. We found all chlorophyll-protein complexes of maize to be present. However, the minor chlorophyll a/b-proteins CP29 and CP26, and to a greater extent CP24 and the major light-harvesting complex II were reduced relative to the photosystem (PS) II core-complex. Also the chlorophyll a/b-antennae of PSI were reduced relative to the reaction-centre polypeptides. When isolated by flatbed isoelectrofocussing, the chlorophyll-a/b complexes of PSII showed a higher chlorophyll-a/b ratio and a lower ratio of chlorophyll to protein than the same complexes from continuous light; additionally, they bound more carotenoids per protein than the latter. Thus the altered organization of the photosynthetic apparatus of plants from intermittent light is caused by two different factors: (i) the altered stoichiometry of chlorophyll-binding proteins and (ii) a different ratio of pigment to protein within individual chlorophyll-proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00199759
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  • 10
    Electronic Resource
    Electronic Resource
    Isolation and characterization of chloroplast Photosystem II antenna of spinach by reversed-phase liquid chromatography (1999)
    Springer
    Photosynthesis research 61 (1999), S. 281-290 
    Details
    ISSN: 1573-5079
    Keywords: antenna system ; chlorophyll–proteins ; HPLC ; LHC II ; Photosystem II ; spinach
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The protein components of the Photosystem II antenna system, isolated from spinach thylakoids, have been resolved by reversed-phase high performance liquid chromatography (RP-HPLC) using a butyl-silica stationary phase packed either into analytical or semi-preparative columns. Peak identification has been accomplished by a combination of various SDS–PAGE systems employing either Comassie (or silver) staining or immunological detection using polyclonal antibodies raised against LHC II and against CP29, CP26 and CP24 proteins and by aminoacid microsequence. Moreover, peak identification is consistent with the molecular masses determined by Electrospray Ionization Mass Spectrometry (HPLC-ESI-MS). The developed RP-HPLC method allows the resolution of all the protein components of the Photosystem II major Light Harvesting Complex (LHC II) and minor PS II antenna complex (CP24, CP26 and CP29) from grana membranes (BBY) and estimation of their relative stoichiometry in natural and stressed conditions, avoiding the expensive and time consuming separation procedure by sucrose-gradient ultracentrifugation and isoelectrofocusing.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006397419473
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