English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/157263
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE
Exportar a otros formatos:


Probing nergy landscapes of cytochrome b6f with spectral hole burning: Effects of deuterated solvent and detergent

AuthorsLevenberg, Alexander; Shafiei, Golia; Luján Serrano, María Ángeles CSIC ORCID ; Giannacopoulos, Steven; Picorel Castaño, Rafael CSIC ORCID ; Zazubovich, Valter
Issue DateSep-2017
CitationLevenberg A, Shafiei G, Luján MA, Giannacopoulos S, Picorel R, Zazubovich V. Probing nergy landscapes of cytochrome b6f with spectral hole burning: Effects of deuterated solvent and detergent. Journal of Physical Chemistry B 121 (42): 9848-9858 (2017)
AbstractIn non-photochemical spectral hole burning (NPHB) and spectral hole recovery experiments, cytochrome b6f protein exhibits behavior that is almost independent of the deuteration of the buffer/glycerol glassy matrix containing the protein, apart from some differences in heat dissipation. On the other hand, strong dependence of the hole burning properties on sample preparation procedures was observed and attributed to a large increase of the electron–phonon coupling and shortening of the excited-state lifetime occurring when n-dodecyl β-d-maltoside (DM) is used as a detergent instead of n-octyl β-d-glucopyranoside (OGP). The data was analyzed assuming that the tunneling parameter distribution or barrier distribution probed by NPHB and encoded into the spectral holes contains contributions from two nonidentical components with accidentally degenerate excited state λ-distributions. Both components likely reflect protein dynamics, although with some small probability one of them (with larger md2) may still represent the dynamics involving specifically the −OH groups of the water/glycerol solvent. Single proton tunneling in the water/glycerol solvent environment or in the protein can be safely excluded as the origin of observed NPHB and hole recovery dynamics. The intensity dependence of the hole growth kinetics in deuterated samples likely reflects differences in heat dissipation between protonated and deuterated samples. These differences are most probably due to the higher interface thermal resistivity between (still protonated) protein and deuterated water/glycerol outside environment.
Description36 Pags.- 9 Figs. The definitive version is available at: http://pubs.acs.org/journal/jpcbfk
Publisher version (URL)http://dx.doi.org/10.1021/acs.jpcb.7b07686
Appears in Collections:(EEAD) Artículos
Files in This Item:
File Description SizeFormat 
PicorelR_JPhysChemB_2017.pdf907,3 kBAdobe PDFThumbnail
Show full item record
Review this work

Related articles:

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.