0000000000435404
AUTHOR
Margus Rätsep
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…
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…
Red Spectral Forms of Chlorophylls in Green Plant PSI - A Site-Selective and High-Pressure Spectroscopy Study
One of the special spectroscopic characteristics of photosystem I (PSI) complexes is that they possess absorption and emission bands at lower energy than those of the reaction center. In this paper, the red pigment pools of PSI-200, PSI-core, and LHCI complex from Arabidopsis thaliana have been characterized at low temperatures by means of spectrally selective (hole-burning and fluorescence line-narrowing) and high-pressure spectroscopic techniques. It was shown that the green plant PSI-200 complex has at least three red pigment pools, from which two are located in the PSI-core and one, in the peripheral light-harvesting complex I (LHCI). All of the red pigment pools are characterized by st…