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Near edge X-ray absorption fine structure spectroscopy (NEXAFS) of pigment-protein complexes : peridinin- chlorophyll a-protein (PCP) of Amphidinium carterae

  • Peridinin-chlorophyll a protein (PCP) is a unique water soluble antenna complex that employs the carotenoid peridinin as the main light-harvesting pigment. In the present study the near edge X-ray absorption fine structure (NEXAFS) spectrum of PCP was recorded at the carbon Kedge. Additionally, the NEXAFS spectra of the constituent pigments, chlorophyll a and peridinin, were measured. The energies of the lowest unoccupied molecular levels of these pigments appearing in the carbon NEXAFS spectrum were resolved. Individual contributions of the pigments and the protein to the measured NEXAFS spectrum of PCP were determined using a "building block" approach combining NEXAFS spectra of the pigments and the amino acids constituting the PCP apoprotein. The results suggest that absorption changes of the pigments in the carbon near K-edge region can be resolved following excitation using a suitable visible pump laser pulse. Consequently, it may be possible to study excitation energy transfer processes involving "optically dark" states ofPeridinin-chlorophyll a protein (PCP) is a unique water soluble antenna complex that employs the carotenoid peridinin as the main light-harvesting pigment. In the present study the near edge X-ray absorption fine structure (NEXAFS) spectrum of PCP was recorded at the carbon Kedge. Additionally, the NEXAFS spectra of the constituent pigments, chlorophyll a and peridinin, were measured. The energies of the lowest unoccupied molecular levels of these pigments appearing in the carbon NEXAFS spectrum were resolved. Individual contributions of the pigments and the protein to the measured NEXAFS spectrum of PCP were determined using a "building block" approach combining NEXAFS spectra of the pigments and the amino acids constituting the PCP apoprotein. The results suggest that absorption changes of the pigments in the carbon near K-edge region can be resolved following excitation using a suitable visible pump laser pulse. Consequently, it may be possible to study excitation energy transfer processes involving "optically dark" states of carotenoids in pigment-protein complexes by soft X-ray probe optical pump double resonance spectroscopy (XODR).show moreshow less

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Metadaten
Author:Herbert Legall, Holger Stiel, Michael Beck, Dieter Leupold, Wieslaw I. Gruszecki, Heiko Lokstein
URL:http://www.sciencedirect.com/science/journal/0165022X
DOI:https://doi.org/10.1016/j.jbbm.2006.08.005
ISSN:0165-022X
Document Type:Article
Language:English
Year of first Publication:2007
Year of Completion:2007
Release Date:2017/03/24
Source:Journal of biochemical and biophysical methods. - ISSN 0165-022X. - 70 (2007), 3, S. 369 - 376
Organizational units:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie
Peer Review:Referiert