Nouvelle synthese de precurseurs phenoliques des lignines utilisant les sels d'iminium des acides p-hydroxy cinnamiques

Duran, E.; Gorrichon, Liliane; Cazaux, Louis; Tisnès, P.

doi:10.1016/s0040-4039(01)81282-x

Cited by 18 publications

(12 citation statements)

References 12 publications

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“…Crystal structure of the hydrated crystal of the PYP model : The model chromophore 1 was prepared11 by reacting 2‐fluoro‐1‐methylpyiridinium, para ‐hydroxycinnamic acid and thiophenol, and purified by column chromatography (the synthetic procedure is detailed in the Experimental Section). Our repeated attempts to crystallize 1 by using several crystallization methods and various conditions, which extended over a couple of years, always resulted in white or pale‐yellow powders.…”

Section: Resultsmentioning

confidence: 99%

Visible‐Light‐Induced Photodimerization of a Photoactive Yellow Protein (PYP) Chromophore Model in a Single Crystal

Nath¹,

Manoj²,

Gâz³

et al. 2013

Chemistry A European J

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The chromophore of the photoactive yellow protein (PYP), the photoreceptor in the photomotility of the bacterium Halorhodospira halophila, is a deprotonated para-coumaric thioester linked to the side residue of a cysteine residue. The photophysics of the PYP chromophore is conveniently modeled with para-hydroxycinnamic thiophenyl esters. Herein, we report the first direct evidence, obtained with X-ray diffraction, of photodimerization of a para-hydroxycinnamic thiophenyl ester in single crystalline state. This result represents the first direct observation of [2+2] dimerization of a model PYP chromophore, and demonstrates that even very weak light in the visible region is capable of inducing parallel radical reactions in PYP from the excited state of the chromophore, in addition to the main reaction pathway (trans-cis isomerization). This PYP model system adds an interesting example to the known solid-state photodimerizations, because unlike the anhydrous crystal (which is not capable of sustaining the stress and disintegrates in the course of photodimerization), a single water molecule "dilutes" the structure to the extent sufficient for single-crystal-to-single-crystal reaction.

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Section: Resultsmentioning

confidence: 99%

Visible‐Light‐Induced Photodimerization of a Photoactive Yellow Protein (PYP) Chromophore Model in a Single Crystal

Nath¹,

Manoj²,

Gâz³

et al. 2013

Chemistry A European J

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“…The antibacterial substance was eluted as a single symmetrical peak without impurity, as detected by UV absorbance at 220 nm. The amount of antibacterial substance was determined by the method of Lowry et al [17], with 4‐hydroxycinnamic acid as the standard. All of the HPLC procedures were carried out using a HP 1050 HPLC system (Hewlett‐Packard, California, USA).…”

Section: Methodsmentioning

confidence: 99%

Isolation of p‐hydroxycinnamaldehyde as an antibacterial substance from the saw fly, Acantholyda parki S

et al. 1999

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We purified an antibacterial substance from larvae of the saw fly, Acantholyda parki S., and identified its molecular structure as p-hydroxycinnamaldehyde. We then synthesized it by reduction of p-hydroxycinnamic acid. The antibacterial activity of the synthetic p-hydroxycinnamaldehyde was equal to that of the authentic substance. This molecule was found to have a broad antibacterial spectrum against not only Gram-negative, but also Gram-positive bacteria. Furthermore, it showed antifungal activity against Candida albicans. We suggest that this substance may play a role in the defense system of this insect. This is the first report of p-hydroxycinnamaldehyde of animal origin.z 1999 Federation of European Biochemical Societies.

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“…The model compound, 4-hydroxycinnamyl phenyl thioester (HCPT), was prepared by the reaction of thiophenol with acyloxypyridinium salt formed from free 4-hydroxycinnamic acid and 2-fluoro-1 -methylpyridinium p-toluenesulfonate, as described previously (Duran et al, 1987). The final purification of the model compound was performed with a Rainin HPLC, which was equipped with a C18 reverse phase column (25 mm x 500 mm) run with a linear gradient from 60% acetonitrile in water to 100% acetonitrile over 40 min at 4.0 mL, min-'.…”

Section: Methodsmentioning

confidence: 99%

Resonance Raman evidence that the thioester-linked 4-hydroxycinnamyl chromophore of photoactive yellow protein is deprotonated

Kim

Mathies²,

Hoff³

et al. 1995

Biochemistry

135

187

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Resonance Raman evidence that the thioester-linked 4-hydroxycinnamoyl chromophore of photoactive yellow protein is deprotonated in the dark state. Kim, M.; Mathies, R.A.; Hoff, W.D.; Hellingwerf, K.J. Published in: Biochemistry DOI:10.1021/bi00039a024Link to publication Citation for published version (APA):Kim, M., Mathies, R. A., Hoff, W. D., & Hellingwerf, K. J. (1995). Resonance Raman evidence that the thioesterlinked 4-hydroxycinnamoyl chromophore of photoactive yellow protein is deprotonated in the dark state. Biochemistry, 34, 12669-12672. DOI: 10.1021/bi00039a024 General rightsIt is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), other than for strictly personal, individual use, unless the work is under an open content license (like Creative Commons). Disclaimer/Complaints regulationsIf you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: http://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. ABSTRACT: Resonance Raman spectra of the ground state of photoactive yellow protein (PYP), a photoactive pigment found in Ectothiorhodospira halophila, have been obtained with excitation at 413.1 nm using a microspinning sample cell. The resonance Raman spectra of the thioester-linked 4-hydroxycinnamyl chromophore in the protein are compared with the preresonance Raman spectra of the 4-hydroxycinnamyl phenyl thioester and 4-hydroxycinnamic acid model compounds at various pH values. Bands at 1568, 1542, 1500, 1434, and 1166 cm-' in the Raman spectrum of the anionic form of the 4-hydroxycinnamyl phenyl thioester are shown to be characteristic for the deprotonation of the chromophore. The observation of bands in PYP exhibiting very similar frequency and intensity patterns provides strong evidence that the chromophore in PYP is stabilized as a phenolate anion at pH 7.4, in support of conclusions from crystallographic studies. Furthermore, the insensitivity of the PYP Raman spectrum to placement of the protein in D20 buffer is consistent with the absence of the exchangeable phenolic proton on the cinnamyl chromophore. These results establish the feasibility of elucidating the molecular mechanism of light-toinformation transduction by this new photosensory pigment with resonance Raman spectroscopy.Photoactive yellow protein (PYP),' a water-soluble yellowcolored protein with a visible absorption maximum at 446 nm, is found in several halophilic phototrophic bacteria including Ectothiorhodospira halophila (Meyer, 1985;Meyer et al., 1990;Hoff et al., 1994~). E. halophila exhibits a negative phototactic reaction or repellent response to physiological intensiti...

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Nouvelle synthese de precurseurs phenoliques des lignines utilisant les sels d'iminium des acides p-hydroxy cinnamiques

Cited by 18 publications

References 12 publications

Visible‐Light‐Induced Photodimerization of a Photoactive Yellow Protein (PYP) Chromophore Model in a Single Crystal

Visible‐Light‐Induced Photodimerization of a Photoactive Yellow Protein (PYP) Chromophore Model in a Single Crystal

Isolation of p‐hydroxycinnamaldehyde as an antibacterial substance from the saw fly, Acantholyda parki S

Resonance Raman evidence that the thioester-linked 4-hydroxycinnamyl chromophore of photoactive yellow protein is deprotonated

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