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Primary photoprocesses in oxyblepharismin interacting with its native protein partner
- Source :
- Journal of photochemistry and photobiology. A, Chemistry, 185 (2007): 345–353. doi:10.1016/j.jphotochem.2006.06.030, info:cnr-pdr/source/autori:Mahet M.; Plaza P.; Martin M. M.; Checcucci G.; Lenci F./titolo:Primary photoprocesses in oxyblepharismin interacting with its native protein partner/doi:10.1016%2Fj.jphotochem.2006.06.030/rivista:Journal of photochemistry and photobiology. A, Chemistry (Print)/anno:2007/pagina_da:345/pagina_a:353/intervallo_pagine:345–353/volume:185, Journal of Photochemistry and Photobiology A: Chemistry, Journal of Photochemistry and Photobiology A: Chemistry, Elsevier, 2007, 185, pp.345. ⟨10.1016/j.jphotochem.2006.06.030⟩
- Publication Year :
- 2007
- Publisher :
- Elsevier Sequoia, Lausanne , Svizzera, 2007.
-
Abstract
- The primary photoprocesses in the photoreceptor for the step-up photophobic response of the light-adapted cells of Blepharisma japonicum (OBIP, OxyBlepharismin bInding Protein) have been studied by ultrafast UV–vis transient spectroscopy. The results are rationalized in terms of heterogeneity of the OBIP sample. Two independent classes of chromoprotein are proposed: a “reactive” species, which presents a specific 680-nm band decaying in 4 and 56 ps and a “non-reactive” one, which behaves like the free chromophore (OxyBP) in solution. A bimolecular photooxidation of OxyBP in the presence of 1,4-benzoquinone was performed to record the absorption spectrum of the OxyBP radical cation. Comparison with reactive OBIP suggests that an electron transfer could be involved in the primary photoprocesses of OBIP and possibly trigger the sensory transduction chain of B. japonicum . In addition, the specificity of the chromophore–protein interaction was investigated by studying the artificial complex that OxyBP forms with human serum albumin (HSA). OxyBP–HSA happens to be spectroscopically much closer to free OxyBP than to OBIP. This highlights the specific nature of the interaction between OxyBP and its native protein partner and further supports the proposal that OBIP is the actual photoreceptor for the photophobic response of B. japonicum .
- Subjects :
- General Chemical Engineering
General Physics and Astronomy
010402 general chemistry
Photochemistry
01 natural sciences
Photoinduced electron transfer
Electron transfer
Chromoprotein
medicine
Ultrafast transient absorption spectroscopy
ComputingMilieux_MISCELLANEOUS
Human serum albumin (HSA)
biology
010405 organic chemistry
Chemistry
Binding protein
Blepharisma japonicum
Oxyblepharismin
General Chemistry
Chromophore
biology.organism_classification
Human serum albumin
Oxyblepharismin binding protein (OBIP)
0104 chemical sciences
[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry
Radical ion
medicine.drug
Subjects
Details
- ISSN :
- 10106030
- Database :
- OpenAIRE
- Journal :
- Journal of photochemistry and photobiology. A, Chemistry, 185 (2007): 345–353. doi:10.1016/j.jphotochem.2006.06.030, info:cnr-pdr/source/autori:Mahet M.; Plaza P.; Martin M. M.; Checcucci G.; Lenci F./titolo:Primary photoprocesses in oxyblepharismin interacting with its native protein partner/doi:10.1016%2Fj.jphotochem.2006.06.030/rivista:Journal of photochemistry and photobiology. A, Chemistry (Print)/anno:2007/pagina_da:345/pagina_a:353/intervallo_pagine:345–353/volume:185, Journal of Photochemistry and Photobiology A: Chemistry, Journal of Photochemistry and Photobiology A: Chemistry, Elsevier, 2007, 185, pp.345. ⟨10.1016/j.jphotochem.2006.06.030⟩
- Accession number :
- edsair.doi.dedup.....bb17f3fea6e5064bdf4c47a7143effb8