Der UV-Sehfarbstoff der Insekten: Photochemie in vitro und in vivo

Schwemer, Joachim; Gogala, Matija; Hamdorf, Kurt

doi:10.1007/bf00335261

Cited by 31 publications

(2 citation statements)

References 17 publications

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“…Like in cephalopods, the acid metarhodopsin of owlfly is converted to an alkaline form upon raising the pH (pAT = 9.2). This has prompted the suggestion that the binding of the chromophore to the opsin in acid metarhodopsin occurs via a protonated Schiff base linkage which deprotonates upon the formation of alkaline metarhodopsin (Schwemer et al, 1971).…”

Section: Resultsmentioning

confidence: 99%

Resonance Raman spectroscopy of an ultraviolet sensitive insect rhodopsin

Pande¹,

Deng²,

Rath³

et al. 1987

Biochemistry

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We present the first visual pigment resonance Raman spectra from the UV-sensitive eyes of an insect, Ascalaphus macaronius (owlfly). This pigment contains 11-cis-retinal as the chromophore. Raman data have been obtained for the acid metarhodopsin at 10 degrees C in both H2O and D2O. The C = N stretching mode at 1660 cm-1 in H2O shifts to 1631 cm-1 upon deuteriation of the sample, clearly showing a protonated Schiff base linkage between the chromophore and the protein. The structure-sensitive fingerprint region shows similarities to the all-trans-protonated Schiff base of model retinal chromophores, as well as to the octopus acid metarhodopsin and bovine metarhodopsin I. Although spectra measured at -100 degrees C with 406.7-nm excitation, to enhance scattering from rhodopsin (lambda max 345 nm), contain a significant contribution from a small amount of contaminants [cytochrome(s) and/or accessory pigment] in the sample, the C = N stretch at 1664 cm-1 suggests a protonated Schiff base linkage between the chromophore and the protein in rhodopsin as well. For comparison, this mode also appears at approximately 1660 cm-1 in both the vertebrate (bovine) and the invertebrate (octopus) rhodopsins. These data are particularly interesting since the absorption maximum of 345 nm for rhodopsin might be expected to originate from an unprotonated Schiff base linkage. That the Schiff base linkage in the owlfly rhodopsin, like in bovine and in octopus, is protonated suggests that a charged chromophore is essential to visual transduction.

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Section: Resultsmentioning

confidence: 99%

Resonance Raman spectroscopy of an ultraviolet sensitive insect rhodopsin

Pande¹,

Deng²,

Rath³

et al. 1987

Biochemistry

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“…Consequently, prolonged monochromatic light illumination results in a rhodopsin to metarhodopsin ratio that strongly depends on the light wavelength. UV light causes a high metarhodopsin content, and blue light results in a virtually pure rhodopsin content (SCHWEMER et al 1971).…”

Section: Introductionmentioning

confidence: 99%

The dynamics of light adaptation in Ascalaphus (Libelloides macaronius; Neuroptera)

Meglič,

Škorjanc,

Zupančič

2007

ABS

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The owl-fl y or Ascalaphus (Libelloides macaronius; Neuroptera) is an insect with a UV-sensitive superposition eye. Although optical superposition is mainly a feature of dusk/dark active animals, this is a predator living and hunting in bright sunlight. In such conditions the process of light adaptation is believed to be very important, yet it has so far only been partially explored in the owl-fly. Here we present physiological evidence for the migration of the screening pigment, which functions as a light control mechanism. The process of light adaptation was studied optically by dynamic imaging and optical refl ection spectroscopy of the eye-glow. Weestablished that the eye-glow is reduced uniformly upon illumination and that its diameter doesn’t get smaller, which is indicative of pigment migration in the primary pigment cells. The change in spectral absorbance of the dorso-frontal eye is very similar to the absorbance spectrum of the primary pigment cell screening pigment. We found that the change in the light screening due toadaptation is rather small – no more than 10 fold for a 10000 fold change in light intensity. We also found that the rate of adaptation is light-sensitive. We propose that a signifi cant part of this light sensitivity is due to indirect heating of the eye and to the very steep temperature dependency of the rate of adaptation between 30 and 35°C.

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Visual Pigments of Invertebrates

Stavenga

Schwemer

1984

Photoreception and Vision in Invertebrates

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Der UV-Sehfarbstoff der Insekten: Photochemie in vitro und in vivo

Cited by 31 publications

References 17 publications

Resonance Raman spectroscopy of an ultraviolet sensitive insect rhodopsin

Resonance Raman spectroscopy of an ultraviolet sensitive insect rhodopsin

The dynamics of light adaptation in Ascalaphus (Libelloides macaronius; Neuroptera)

Visual Pigments of Invertebrates

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