2D Spectroscopy Study of Water-Soluble Chlorophyll-Binding Protein from Lepidium virginicum

Jan Alster, Heiko Lokstein, Jakub Dostal, Akira Uchida, Donatas Zigmantas

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Water-soluble chlorophyll-binding proteins (WSCPs) are interesting model systems for the study of pigment-pigment and pigment-protein interactions. While class IIa WSCP has been extensively studied by spectroscopic and theoretical methods, a comprehensive spectroscopic study of class IIb WSCP was lacking so far despite the fact that its structure was determined by X-ray crystallography. In this paper, results of two-dimensional electronic spectroscopy applied to the class IIb WSCP from Lepidium virginicum are presented. Global analysis of 2D data allowed determination of energy levels and excitation energy transfer pathways in the system. Some additional pathways, not present in class IIa WSCP, were observed. The data were interpreted in terms of a model comprising two interacting chlorophyll dimers. In addition, oscillatory signals were observed and identified as coherent beatings of vibrational origin.
Original languageEnglish
Pages (from-to)3524-3531
JournalThe Journal of Physical Chemistry Part B
Issue number13
Publication statusPublished - 2014

Bibliographical note

The information about affiliations in this record was updated in December 2015.
The record was previously connected to the following departments: Chemical Physics (S) (011001060)

Subject classification (UKÄ)

  • Atom and Molecular Physics and Optics


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