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  • 1
    Keywords: Photosynthesis-Congresses. ; Electronic books.
    Description / Table of Contents: Proceedings of the XIth International Congress on Photosynthesis.
    Type of Medium: Online Resource
    Pages: 1 online resource (4476 pages)
    Edition: 1st ed.
    ISBN: 9789401139533
    DDC: 572/.46
    Language: English
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  • 2
    ISSN: 1432-2048
    Keywords: Chlororespiration ; Cytochrome c 553 ; Electrochromism ; Photosynthesis ; Plastocyanin ; Pleurochloris
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract For characterisation of chlororespiration in the chlorophyll c-containing alga Pleurochloris meiringensis, we measured the flash-induced electrochromic absorbance changes between 470 and 545 nm and the redox changes of cytochrome f and cytochrome c 553. Cytochrome c 553 was shown to be present in high amounts (1 mol cytochrome c 553 per 300 mol chlorophyll) in this alga and to function as the obligate electron donor for photosystem I instead of plastocyanin. Whereas salicylhydroxamic acid had no effect on the flash-induced absorbance transients, cyanide enhanced the slow-rising (t1/2≈10 ms) kinetic component of the electrochromic absorbance change. Cyanide also accelerated the re-reduction of the cytochrome f +/c 553 + electron pool following the photooxidation by repetitive single-turnover flashes. These data suggest that an oxidase competes with the cytochromes for electrons. The KCN concentration needed to induce these effects was 0.25 mM at half-saturation, whereas mitochondrial respiration was completely blocked at 0.1 mM. Therefore, the oxidase cannot be identical to the cytochrome aa3-oxidase of mitochondria and is most likely located in the chloroplast of P. meiringensis.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Photosynthesis research 43 (1995), S. 49-56 
    ISSN: 1573-5079
    Keywords: Xanthophyceae ; Chl-c-containing algae ; carotenoids ; electrochromic absorbance changes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Flash-induced absorbance changes were measured in the Chl-c-containing alga Pleurochloris meiringensis (Xanthophyceae) between 430 and 570 nm. In addition to the bands originating from redox changes of cytochromes, three major positive and tow negative transient bands were observed both 0.7 and 20 ms after the exciting flash. These transient bands peaking at 520, 480 and 451 nm and 497 and 465 nm, respectively, could be assigned to an almost homogeneous shift of the absorbance bands with maxima at 506, 473 and 444 nm, respectively. The shape of the absorbance transients elicited from PS I or PS II was identical, and the two photosystems contributed nearly equally to the absorbance changes. Furthermore, the decay transients were sensitive to the preillumination of the cells. These data strongly suggest that the absorbance transients originate from an electrochromic response of carotenoid molecules. The pigment species responsible for the 506 nm absorption band, probably heteroxanthin or diatoxanthin, transferred excitation energy to both photosystems as shown by the aid of 77 K fluorescence excitation spectra.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Photosynthesis research 11 (1987), S. 15-27 
    ISSN: 1573-5079
    Keywords: intact chloroplasts ; electrochromic absorbance change ; energization of thylakoids ; transmembrane electric field and ΔpH
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We investigated the frequency-dependence of the flash-induced electrochromic absorbance change, ΔA515, and of the pH-indicating absorbance change of neutral red in isolated intact chloroplasts. The energization pattern of thylakoids depended strongly on the frequency (f) of the exciting flashes, tested between 0.05 and 2 s−1. When the frequency was increased from 0.1 to 1 s−1 the total initial change and the slow rise of ΔA515 decreased by about 30% and 70%, respectively, and both the slow rise and decay were considerably accelerated. These changes were fully reversible, even after prolonged excitation at 1 s−1, if the frequency was decreased again to 0.1 s−1. Accumulation of an appreciable transmembrane electric field strength could not be detected in any of our experiments, at high frequency, since the decay of ΔA515 was considerably accelerated when the frequency was increased. In contrast, ΔpH significantly increased at higher frequencies of the exciting flashes. In the steady-state (after about 100 flashes) ΔpH was about 0.5–0.8 pH unit higher than in the dark or at low frequencies. In the presence of nigericin or dithionite, both of which prevented accumulation of protons in the lumen, the total initial change in ΔA515 at f=1 s−1 relative to that at f=0.1 s−1 decreased to a similar extent as in the control. The proportion of the slow rise relative to the initial amplitude, however, did not decrease. Our data support the suggestion that ΔpH controls the amplitude of the slow rise of ΔA515. However, contrary to a previous statement (B. Bouges-Bouquet (1981) Biochim. Biophys. Acta 535, 327–340), we show that the ΔpH effect cannot be accounted for by variation of the rate of this kinetic component of ΔA515.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1573-5079
    Keywords: chiral macroorganization ofchromophores ; circular dichroism ; chlorophyllfluorescence induction ; photoinhibition ofphotosynthesis ; spinach thylakoids
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We investigated the effect of photoinhibitory illumination on the chiral macroorganization of the chromophores in spinach thylakoid membranes. By measuring circular dichroism (CD), we found that prolonged (15 min) illumination of membranes with intense white light led to irreversible diminishment of the main CD bands originating from the chiral macroorganization of the chromophores. The irreversible decrease of the main CD bands showed a nearly linear correlation with the extent of photoinhibition which was determined by chlorophyll fluorescence induction. CD measurements also revealed that the excitonic CD bands, which are given rise by short-range interactions between the chromophores inside the complexes or particles, were largely insensitive to the photoinhibitory illumination of the membranes. These data show that, whereas photoinhibitory treatment has no perceptible effect on the molecular architecture of the bulk of the pigment–protein complexes, it leads to a disorganization of their macroarray, and an irreversible disassembly of the chirally organized macrodomains.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1573-5079
    Keywords: algae ; reconstitution ; light-harvesting complex ; circular dichroism ; pigment-pigment interaction ; protein secondary structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Earlier we have shown by in vitro reconstitution experiments that the pigment composition of the chlorophyll alb-binding light-harvesting complex of the green alga Chlorella fusca could be altered in a relatively broad range (Meyer and Wilhelm 1993). In this study we used these reconstituted complexes of different pigment loading to analyze the excitonic interactions between the pigment molecules and the secondary structure by means of circular dichroism spectra in the visible and the far UV spectral regions, respectively. We found that, in contrast to the expectations, the pigment composition and pigment content hardly affected the circular dichroism spectra in the visible spectral region. Reconstituted complexes, independent of their pigment composition, exhibited the most characteristic circular dichroism bands of the native light-harvesting complex, even if one polypeptide bound only 3 chlorophyll a, 3 chlorophyll b and 1–2 xanthophyll molecules. Full restoration of the protein secondary structure, however, could not be achieved. The α-helix content depended significantly on the pigment composition as well as on the pigment-protein ratio of the reconstituted complexes. Further binding of pigments resulted in restoration of the minor excitonic circular dichroism bands, the amplitudes of which depended on the pigment content of the reconstituted complexes. These data suggest that in the reconstitution of light-harvesting complexes a ‘central cluster’ of pigment molecules plays an important role. Further binding of pigments to the ‘peripheral binding sites’ appeared also to stabilize the protein secondary structure of the reconstituted complexes.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1573-5079
    Keywords: antimycin ; circular dichroism ; light-harvesting chlorophyll a/b complex (LHC II) ; light-induced structural changes ; ΔpH ; thermooptic effect
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We investigated the temperature dependence and inhibitor sensitivity of the light-induced reversible changes in the circular dichroism (ΔCD) of chloroplast thylakoid membranes. Earlier, these changes, which originate from structural changes affecting the chiral macroorganization of the chromophores, were thought to be driven by photochemically generated proton and/or ion gradients in the thylakoids [Garab et al. (1988) Biochemistry 27: 2430]. However, more recently, these changes have been shown to be largely independent of the photochemical activity of thylakoids, and ΔCD has been observed in lamellar aggregates of the light harvesting chlorophyll a/b complex (LHC II) of Photosystem II [Barzda et al. (1996) Biochemistry 35: 8981]. Here, we show that in thylakoids (i) ΔCD is gradually and substantially decelerated upon gradually decreasing the temperature from 33 °C to 2 °C, and abruptly disappears above 35–37 °C; (ii) ΔCD is inhibited with nigericin with I50≈ 1 μM, which is about 10 times higher than the I50for the transmembrane ΔpH; (iii) ΔCD can be inhibited with dicyclohexylcarbodiimide that blocks proton binding at the lumenal side of LHC II; (iv) quinone antagonists, such as antimycin-A and myxothiazol, inhibit ΔCD without noticeably affecting the electron and proton transport, and the chiral macroorganization of the chromophores in the dark. We conclude that ΔCD is conditioned but not driven by the photochemical activity of the membranes, and the structural changes are given rise by a physical mechanism previously unrecognized in thylakoids, thermooptic effect described for liquid crystals. We discuss the possible link between the deactivation(s) of the excess excitation energy and ΔCD, the light-induced changes in the chiral macroorganization of the chromophores of the photophysical apparatus in thylakoids.
    Type of Medium: Electronic Resource
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