0000000000435406
AUTHOR
Jörg Pieper
Excitonic energy level structure and pigment-protein interactions in the recombinant water-soluble chlorophyll protein. II. Spectral hole-burning experiments.
Persistent spectral hole burning at 4.5 K has been used to investigate the excitonic energy level structure and the excited state dynamics of the recombinant class-IIa water-soluble chlorophyll-binding protein (WSCP) from cauliflower. The hole-burned spectra are composed of four main features: (i) a narrow zero-phonon hole (ZPH) at the burn wavelength, (ii) a number of vibrational ZPHs, (iii) a broad low-energy hole at ~665 and ~683 nm for chlorophyll b- and chlorophyll a-WSCP, respectively, and (iv) a second satellite hole at ~658 and ~673 nm for chlorophyll b- and chlorophyll a-WSCP, respectively. The doublet of broad satellite holes is assigned to an excitonically coupled chlorophyll dim…
QENS investigation of filled rubbers
The polymer segmental dynamics is investigated in a series of silica-filled rubbers. The presence of inert fillers in polymers greatly affects the mechanical and physical performance of the final materials. For example, silica has been proposed as a reinforcing agent of elastomers in tire production. Results from quasielastic neutron scattering and Dynamic Mechanical Thermal Analysis (DMTA) measurements are presented on styrene–ran-butadiene rubber filled with silica. A clear indication is obtained of the existence of a bimodal dynamics, which can be rationalized in terms of the relaxation of bulk rubber and the much slower relaxation of the rubber adsorbed on the filler surface.
Excitonic Energy Level Structure and Pigment−Protein Interactions in the Recombinant Water-Soluble Chlorophyll Protein. I. Difference Fluorescence Line-Narrowing
Difference fluorescence line-narrowing spectroscopy at 4.5 K was employed to investigate electron-phonon and electron-vibrational coupling strengths of the lower exciton level of water-soluble chlorophyll-binding protein (WSCP) from cauliflower reconstituted with chlorophyll a or chlorophyll b, respectively. The electron-phonon coupling is found to be moderate with integral Huang-Rhys factors S in the order of 0.81-0.85. A weak dependence of S on excitation wavelength within the inhomogeneously broadened fluorescence origin band is attributed to a sizable contribution of nonresonant excitation that varies with excitation wavelength. The strongly asymmetric and highly structured one-phonon p…
Water soluble chlorophyll binding protein of higher plants: A most suitable model system for basic analyses of pigment–pigment and pigment–protein interactions in chlorophyll protein complexes
Abstract This short review paper describes spectroscopic studies on pigment–pigment and pigment–protein interactions of chlorophyll (Chl) a and b bound to the recombinant protein of class IIa water soluble chlorophyll protein (WSCP) from cauliflower. Two Chls form a strongly excitonically coupled open sandwich dimer within the tetrameric protein matrix. In marked contrast to the mode of excitonic coupling of Chl and bacterio-Chl molecules in light harvesting complexes and reaction centers of all photosynthetic organisms, the unique structural pigment array in the Chl dimer of WSCP gives rise to an upper excitonic state with a large oscillator strength. This property opens the way for thorou…
Protein and solvent dynamics of the water-soluble chlorophyll-binding protein (WSCP)
This study presents quasielastic neutron scattering data of the water-soluble chlorophyll-binding protein (WSCP) and the corresponding buffer solution at room temperature. The contributions of protein and buffer solution to the overall scattering are carefully separated. Otherwise, the fast water dynamics dominating the buffer contribution is likely to mask the slow protein dynamics. In the case of WSCP, the protein scattering can be described by two contributions: i) internal protein dynamics represented by a diffusion in a sphere with an average radius of 2.7 u A and ii) global (Brownian) diffusion of the WSCP macromolecule with an upper limit for the translational diffusion coefficient o…