Abstract
The excitation energy transfer between chlorophyll b (Chl b) and chlorophyll a (Chl a) in the isolated trimeric chlorophyll-a/b-binding protein complex of spinach photosystem 2 (LHC II) has been studied by femtosecond spectroscopy. In the main absorption band of Chl b the ground state recovery consists of two components of 0.5 ps and 2.0 ps, respectively. Also in the Chl a absorption band, at 665 nm, the ground state recovery is essentially bi-exponential. In this case is, however, the fastest relaxation lifetime is a 2.0 ps component followed by a slower component with a lifetime in the order of 10–20 ps. In the Chl b absorption band a more or less constant anisotropy of r = 0.2 was observed during the 3 ps the system was monitored. In the Chl a absorption band there was, however, a relaxation of the anisiotropy from r = 0.3 to a quasi steady state level of r = 0.18 in about 1 ps. Since the 0.5 ps component is only seen upon selective excitation of Chl b we assign this component to the energy transfer between Chl b and Chl a. The other components most likely represents redistribution processes of energy among spectrally different forms of Chl a. The energy transfer process between Chl b and Chl a can well be explained by the Förster mechanism which also gives a calculated distance of 13 Å between interacting chromophores. The organisation of chlorophylls in LHC II is discussed in view of the recent crystal structure data (1991) Nature 350, 130].
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.