Linear dichroic spectra and fluorescence polarization of biliverdin

Chae, Quae; Song, Pill‐Soon

doi:10.1021/ja00848a004

Cited by 53 publications

(20 citation statements)

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“…The ratio of the dipolar strengths, D w / b l s (Braslavsky et al, 1980) smaller for the transient absorbance than it is for PI. Based on calculated trend analyses of the conformational influence on the absorption spectra of bilatrienes (Burke er al., 1972;Chae and Song, 1975;Song et al, 1979;Wagnitre and Blauer, 1976) and the phytochrome chromophore (Pasternak andWagnibre, 1979: Sugimoto et al, 1976) we can now suggest, therefore, that the chromophore of lumi-R should have a more extended conformation than that of P,. At 273 K lumi-R did not return to P, since the bleached signal did not recover within I ms (about ten times the lifetime of lumi-R), in accordance with earlier experiences by Linschitz et a/.…”

Section: Results and Dlscussionmentioning

confidence: 77%

Characterization of a Microsecond Intermediate in the Laser Flash Photolysis of Small Phytochrome From Oat

Braslavsky

Matthews

Herbert

et al. 1980

Photochem & Photobiology

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Abstract— Irradiation of small phytochrome from oat in its Pr form with 15 ns laser pulses of different wavelengths(605–655 nm) gave rise to a difference absorption with maxima at 400 and 685 nm for the first detectable transient. Bleaching of a 660 nm band was observed, non‐recuperable up to 1 ms. The transient absorption has a lifetime of 70±15 μs at 273 K. The transient is tentatively identified as lumi‐R and the conformation of its chromophore is postulated to be more extended than that of Pr. A deviation from the exponential decay of the lumi‐R absorption at 284 and 300 K and the lack of observable enhancement of the far‐red absorption within 1 ms are interpreted in terms of the appearance of still other intermediates on this time scale between lumi‐R and Pfr phytochrome.

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Section: Results and Dlscussionmentioning

confidence: 77%

Characterization of a Microsecond Intermediate in the Laser Flash Photolysis of Small Phytochrome From Oat

Braslavsky

Matthews

Herbert

et al. 1980

Photochem & Photobiology

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“…The most important one seems to be the geometry of the chromophore. This has been born out of a series of molecular orbital calculations performed in different laboratories [7][8][9][10][11], and more recently corroborated experimentally [3, 5a, 12-15]. Whereas the cyclic-helical chromophores typical for bile pigments in solution have a low ratio ß A v.s nuv of the intesities of the visible and near-UV absorption bands, this ratio is high in extended chromophores like the ones in native phycocyanins [5 a], and in the neobiliverdins found first in insects [3], and more recently in other invertebrates [16].…”

Section: Pieris Brassicae Biliproteinsmentioning

confidence: 99%

Conformational studies of biliproteins from the insects pieris brassicae and cerura vinula

Scheer¹,

Kayser

1988

Zeitschrift Für Naturforschung C

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Chromophore conformation and protein secondary structure of biliproteins from the butterfly, Pieris brassicae, and the moth. Cerura vinula, have been investigated by absorption, circular dichroism and fluorescence spectroscopy. The chromophore of the P. brassicae protein, biliverdin ΙΧγ, has probably a cyclic-helical structure similar to that of free bile pigments of the biliverdin type. Though achiral by structure the chromophore displays strong optical activity in the native protein-bound state, but becomes inactive after urea denaturation of the protein. A minor biliprotein from P. brassicae shows absorption, circular dichroism and fluorescence spectra identical to the main biliprotein. In the biliprotein from Cerura vinula the structure of the pigment is still unknown. It has a semi-open conformation intermediate between that of the Pieris proteins and that of the phycobiliprotein. C-phycocyanin, and it retains optical activity after urea denaturation. The band widths and the size of the Stokes shifts of the fluorescence spectra indicate a high degree of conformational flexibility of the chromophores in the two Pieris pigments, and a decreased flexibility in the one from Cerura. In the biliproteins from both insects the polypeptides are low in α-helix content compared to that of phycobiliproteins. From these and earlier data, insect and algal biliproteins seem to be related only distantly if at all. but there exist also considerable differences among insect biliproteins from different species.

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“…Kroes (1970) already noted the similarity between the absorption spectra of mesobiliverdin and the chromophore cleaved from phytochrome. Chae and Song (1975) observed that the long-wave absorption maximum of biliverdin shifts over some 57 nm to about 710 nm upon cooling a solution to 77 K. It is, therefore, conceivable that binding of a compound with a biliverdin type structure to a protein could shift the absorption maximum sufficiently to explain the Pfr spectrum (P-S. Song, personal commun.). Recent calculations by Sugimoto (personal commun.)…”

Section: Chemistry Of the Chromophore (A) Chemical Structurementioning

confidence: 99%

Phototransformations of Phytochrome

Kendrick

Spruit

1977

Photochem & Photobiology

155

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Abstract-Phytochrome is the photoreversible chromoprotein that controls many aspects of plant growth and development. Phototransformations of the red absorbing form (Pr) and the far red absorb ing form (Pfr) involve initial photoreactions followed by dark relaxation reactions. Techniques for the study of intermediates of phototransformation and the present picture of intermediates involved in the phototransformations of Pr and Pfr are outlined. The molecular natures of the phototransformations are reviewed in relationship to knowledge of the chemistry of the chromophore and apoprotein. The significance of phytochrome intermediates in understanding the physiology of phytochrome controlled responses is discussed

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Linear dichroic spectra and fluorescence polarization of biliverdin

Cited by 53 publications

References 0 publications

Characterization of a Microsecond Intermediate in the Laser Flash Photolysis of Small Phytochrome From Oat

Characterization of a Microsecond Intermediate in the Laser Flash Photolysis of Small Phytochrome From Oat

Conformational studies of biliproteins from the insects pieris brassicae and cerura vinula

Phototransformations of Phytochrome

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