UV fine structure of the spectral sensitivity of flies visual cells

Gemperlein, R.; Paul, Rüdiger J.; Lindauer, E.; Steiner, Andreas

doi:10.1007/bf00450671

Cited by 27 publications

(12 citation statements)

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“…Such pigments have evolved many times, not only in photosynthetic systems, but also in others. Among others, they occur in photolyases (Fujihashi et al 2007), in vision (Gemperlein et al 1980;Vogt andKirschfeld 1983, Douglas et al 1999), and in light-driven proton pumping (Lanyi and Balashov 2008); further, energy transfer between pigments also takes place in some cases of bioluminescence (Ruby and Nealson 1977;Cormier 1976, 1978;Ward et al 1980). The possibility of extending the spectral range in this way may have made the spectral properties of chlorophyll less critical than they would otherwise have been.…”

Section: Figmentioning

confidence: 92%

A viewpoint: Why chlorophyll a?

et al. 2009

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Chlorophyll a (Chl a) serves a dual role in oxygenic photosynthesis: in light harvesting as well as in converting energy of absorbed photons to chemical energy. No other Chl is as omnipresent in oxygenic photosynthesis as is Chl a, and this is particularly true if we include Chl a(2), (=[8-vinyl]-Chl a), which occurs in Prochlorococcus, as a type of Chl a. One exception to this near universal pattern is Chl d, which is found in some cyanobacteria that live in filtered light that is enriched in wavelengths >700 nm. They trap the long wavelength electronic excitation, and convert it into chemical energy. In this Viewpoint, we have traced the possible reasons for the near ubiquity of Chl a for its use in the primary photochemistry of Photosystem II (PS II) that leads to water oxidation and of Photosystem I (PS I) that leads to ferredoxin reduction. Chl a appears to be unique and irreplaceable, particularly if global scale oxygenic photosynthesis is considered. Its uniqueness is determined by its physicochemical properties, but there is more. Other contributing factors include specially tailored protein environments, and functional compatibility with neighboring electron transporting cofactors. Thus, the same molecule, Chl a in vivo, is capable of generating a radical cation at +1 V or higher (in PS II), a radical anion at -1 V or lower (in PS I), or of being completely redox silent (in antenna holochromes).

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Section: Figmentioning

confidence: 92%

A viewpoint: Why chlorophyll a?

et al. 2009

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“…One observation (Vogt 1983) is that the high UV-sensitivity is much reduced when the fly larvae are reared on a diet deprived of vitamin A, which also reduces the content of the highly fluorescent 3-hydroxy-retinol. The other observation is that the absorbance spectrum of cellular retinol binding protein (CRBP) from rat liver (Ong and Chytil 1978) has a "vibronic fine structure" with peaks within the UV region at 350 and 368 nm, which is very similar to that of the fly photoreceptors (as recorded photometrically and electrophysiologically by Gemperlein et al 1980 andKirschfeld 1984; see also review by Vogt 1989).…”

Section: Introductionmentioning

confidence: 93%

“…A pronounced vibronic fine structure was seen within the range of the 13-band due to the presence of sensitizing pigment. The fine structure was characterised by three sensitivity maxima, at 333, 350 and 369 nm, close to the wavelengths determined by FIS (Fourier Interferometric Stimulation; Gemperlein et al 1980) and to electrophysiological data (Gribakin and Ukhanov 1990), and by two minima, at 339 and 362 nm. The relative sensitivities of the maxima and minima, normalized to 488 nm or 350 nm respectively, are summarised in Table 1.…”

Section: Sensitivity Spectra Of P+ and P--fliesmentioning

confidence: 99%

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Ultra-violet sensitizing pigment in blowfly photoreceptors R1-6; probable nature and binding sites

et al. 1992

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Summary. The spectral sensitivity of photoreceptors R1-6 in the blowfly Calliphora erythrocephala has a characteristic UV fine spectrum due to a sensitizing pigment complexed with the visual pigment, P490. The present study concerns the identity and steric configuration of the sensitizing pigment, and the number of its binding sites on P490.1. Irradiation by "green" light demonstrated that "de novo" synthesis of visual pigment has priority over formation of UV sensitizing pigment, both using the same retinoid pool, and that in absence of sensitizing pigment an aberrant, more thermostable, visual pigment is formed.2. The kinetics of increase in UV sensitivity after application of different retinoids to eyes with low content of P490, and the vibronic UV fine spectrum of the sensitizing pigment, make 13-cis-retinol the most probable candidate for the UV sensitizing pigment or its direct precursor.3. [3-carotene, lutein or zeaxanthin cannot be directly used by the eye as precursors for the UV sensitizing pigment. Vitamin A2 probably is directly coupled to P490. At least two UV sensitizing pigment molecules can complex with P490.4. Artificial UV sensitivity could be induced by the fluorescent thiol probe P-28, probably binding to cysteines 121 and 196 at the extracellular surface of P490.

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“…Consequently, the SSC of a single photoreceptor of a white eye should directly yield the absorption spectrum of the visual pigment. With the spectral scan technique developed during this decade, the SSC can be measured with good resolution and accuracy (Gribakin 1979(Gribakin , 1981(Gribakin , 1988Franceschini 1979;Gemperlein et al 1980;Menzel et al 1986;Paul et al 1986;Kirschfeld et al 1988a). Recently we have found, however, that in snow mutants of the honeybee, SSCs of single photoreceptors are narrower than the absorption spectrum of the visual pigment P526 (Gribakin 1988).…”

Section: Introductionmentioning

confidence: 99%

Is the white eye of insect eye-color mutants really white?

Gribakin

Ukhanov

1990

J Comp Physiol A

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1. Spectral sensitivity curves (SSCs) of (a) the whole eye and peripheral photoreceptors R1-6 were recorded in wild-type flies and chalky mutants of Calliphora, and (b) the whole eye of Drosophila, wild type and mutant white. Our spectrosensitometer provided good resolution and accuracy.2. A vibrational fine structure of the SSC in the ultraviolet spectral range was clearly resolved in all the genotypes studied (Fig. 1).3. In the visible spectral range, the SSCs of whiteeyed mutants appeared to be significantly narrower than the absorption spectrum of the template visual pigments (Fig. 2). The bandwidth ratios (wild type: visual pigment: white-eyed mutant) were as follows: 111_ 10:102:95_4nm and 114+__14"102:93+7 nm in Calliphora whole eye and cells R1-6, respectively; and 118 • 6:100:97___ 2 nm in the whole eye of Drosophila (Fig. 3).4. Long-wave portions of SSCs in mutants showed a good fit with those of the absorption spectrum of visual pigments: P490 for the whole eye, P487 for receptors RI-6 of chalky mutants of Calliphora, and P478 for the whole eye of Drosophila.5. The narrowing of the SSCs compared with the absorption spectrum of the template visual pigment is believed to be due to the presence of hypothetical blueabsorbing pigments in the eye media.

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UV fine structure of the spectral sensitivity of flies visual cells

Cited by 27 publications

References 4 publications

A viewpoint: Why chlorophyll a?

A viewpoint: Why chlorophyll a?

Ultra-violet sensitizing pigment in blowfly photoreceptors R1-6; probable nature and binding sites

Is the white eye of insect eye-color mutants really white?

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