Protein reactivity with singlet oxygen: Influence of the solvent exposure of the reactive amino acid residues
| Autor: | Béatrice Sjöberg, A. Pascu, Mironel Enescu, Angela Staicu, M. L. Pascu, Sarah Foley |
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| Přispěvatelé: | Laboratoire Chrono-environnement ( LCE ), Université Bourgogne Franche-Comté ( UBFC ) -Centre National de la Recherche Scientifique ( CNRS ) -Université de Franche-Comté ( UFC ), National Institute for Laser, Plasma and Radiation Physics ( INFLPR ), National Institute for Laser, Laboratoire Chrono-environnement - CNRS - UBFC (UMR 6249) (LCE), Centre National de la Recherche Scientifique (CNRS)-Université de Franche-Comté (UFC), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC), National Institute for Laser, Plasma and Radiation Physics (INFLPR) |
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Inorganic chemistry Biophysics Tripeptide 010402 general chemistry Photochemistry 01 natural sciences Accessible surface area 03 medical and health sciences chemistry.chemical_compound Reaction rate constant Sasa Radiology Nuclear Medicine and imaging Reactivity (chemistry) Amino Acids chemistry.chemical_classification Radiation Singlet Oxygen Radiological and Ultrasound Technology biology Chemistry Singlet oxygen Tryptophan Proteins biology.organism_classification 0104 chemical sciences Amino acid [CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry Kinetics 030104 developmental biology [ CHIM.THEO ] Chemical Sciences/Theoretical and/or physical chemistry Solvents |
| Zdroj: | Journal of Photochemistry and Photobiology B: Biology Journal of Photochemistry and Photobiology B: Biology, Elsevier, 2016, 159, pp.106. 〈10.1016/j.jphotobiol.2016.03.036〉 Journal of Photochemistry and Photobiology B: Biology, Elsevier, 2016, 159, pp.106. ⟨10.1016/j.jphotobiol.2016.03.036⟩ |
| ISSN: | 1011-1344 |
| DOI: | 10.1016/j.jphotobiol.2016.03.036〉 |
| Popis: | International audience; The singlet oxygen quenching rate constants were measured for three model proteins, bovine serum albumin, β-lactoglobulin and lysozyme. The results were analyzed by comparing them with the corresponding singlet oxygen quenching rate constants for a series of tripeptides with the basic formula GlyAAGly where the central amino acid (AA) was the oxidizable amino acid, tryptophan, tyrosine, methionine and histidine. It was found that the reaction rate constant in proteins can be satisfactorily modelled by the sum of the individual contributions of the oxidizable AA residues corrected for the solvent accessible surface area (SASA) effects. The best results were obtained when the SASA of the AA residues were determined by averaging over molecular dynamics simulated trajectories of the proteins. The limits of this geometrical correction of the AA residue reactivity are also discussed. |
| Databáze: | OpenAIRE |
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