Electronic Structure and Solvation Effects from Core and Valence Photoelectron Spectroscopy of Serum Albumin
| Autor: | Jean-Philippe Renault, Lucie Huart, Aleksandar R. Milosavljević, John D. Bozek, Jerôme Palaudoux, Jean-Michel Guigner, Laurent Marichal, Jocelyne Leroy, Frank Wien, Marie-Anne Hervé Du Penhoat, Christophe Nicolas |
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| Přispěvatelé: | Laboratoire Interdisciplinaire sur l'Organisation Nanométrique et Supramoléculaire (LIONS), Nanosciences et Innovation pour les Matériaux, la Biomédecine et l'Energie (ex SIS2M) (NIMBE UMR 3685), Institut Rayonnement Matière de Saclay (IRAMIS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut Rayonnement Matière de Saclay (IRAMIS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Synchrotron SOLEIL (SSOLEIL), Centre National de la Recherche Scientifique (CNRS), Laboratoire de Chimie Physique - Matière et Rayonnement (LCPMR), Institut de Chimie du CNRS (INC)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Institut de minéralogie, de physique des matériaux et de cosmochimie (IMPMC), Muséum national d'Histoire naturelle (MNHN)-Institut de recherche pour le développement [IRD] : UR206-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Laboratoire Innovation en Chimie des Surfaces et NanoSciences (LICSEN UMR 3685), NanoTheRad strategic Research Initiatives from Paris Saclay University, This work was granted access to the CCRT High-Performance Computing (HPC) facility at CEA under the Grant CCRT2021-Renault, ANR-17-CE30-0017,HighEneCh,Chimie déclenchée par des photons de haute énergie(2017) |
| Rok vydání: | 2022 |
| Předmět: |
X-ray electron spectroscopy
Photoelectron Spectroscopy Organic Chemistry Water Serum Albumin Bovine [CHIM.MATE]Chemical Sciences/Material chemistry General Medicine electronic structure Catalysis theoretical chemistry Computer Science Applications Inorganic Chemistry protein hydration Electronics Physical and Theoretical Chemistry Molecular Biology Serum Albumin Spectroscopy |
| Zdroj: | International Journal of Molecular Sciences International Journal of Molecular Sciences, 2022, 23 (15), pp.8227. ⟨10.3390/ijms23158227⟩ International Journal of Molecular Sciences; Volume 23; Issue 15; Pages: 8227 |
| ISSN: | 1422-0067 1661-6596 |
| DOI: | 10.3390/ijms23158227 |
| Popis: | International audience; X-ray photoelectron spectroscopy of bovine serum albumin (BSA) in a liquid jet is used to investigate the electronic structure of a solvated protein, yielding insight into charge transfer mechanisms in biological systems in their natural environment. No structural damage was observed in BSA following X-ray photoelectron spectroscopy in a liquid jet sample environment. Carbon and nitrogen atoms in different chemical environments were resolved in the X-ray photoelectron spectra of both solid and solvated BSA. The calculations of charge distributions demonstrate the difficulty of assigning chemical contributions in complex systems in an aqueous environment. The high-resolution X-ray core electron spectra recorded are unchanged upon solvation. A comparison of the valence bands of BSA in both phases is also presented. These bands display a higher sensitivity to solvation effects. The ionization energy of the solvated BSA is determined at 5.7 ± 0.3 eV. Experimental results are compared with theoretical calculations to distinguish the contributions of various molecular components to the electronic structure. This comparison points towards the role of water in hole delocalization in proteins. |
| Databáze: | OpenAIRE |
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