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Excitation Wavelength Dependence of the Fluorescence Kinetics in Photosystem I Particles from Synechocystis PCC 6803 and Synechococcus elongatus

Bas Gobets ^*, Ivo H. M. van Stokkum ^*, Frank van Mourik , Jan P. Dekker ^* and Rienk van Grondelle ^*

^* Division of Physics and Astronomy of the Exact Faculty of Sciences and Institute of Molecular Biological Sciences, Vrije Universiteit, Amsterdam, The Netherlands; and Institut de Physique de la Matière Condensée, Université de Lausanne, Lausanne, Switzerland

Correspondence: Address reprint requests to Rienk van Grondelle, Fax: 31-20-444-7899; E-mail: rienk{at}nat.vu.nl.

The excitation-wavelength dependence of the excited-state dynamics of monomeric and trimeric Photosystem I (PSI) particles from Synechocystis PCC 6803 as well as trimeric PSI particles from Synechococcus elongatus has been studied at room temperature using time-resolved fluorescence spectroscopy. For aselective (400 nm), carotenoid (505 nm), and bulk chlorophyll (650 nm) excitation in all species, a downhill energy-transfer component is observed, corresponding to a lifetime of 3.4–5.5 ps. For selective red excitation (702–719 nm) in all species, a significantly faster, an 1-ps, uphill transfer component was recorded. In Synechococcus PSI, an additional 10-ps downhill energy-transfer component is found for all wavelengths of excitation, except 719 nm. Each of the species exhibits its own characteristic trap spectrum, the shape of which is independent of the wavelength of excitation. This trap spectrum decays in 23 ps in both monomeric and trimeric Synechocystis PSI and in 35 ps in trimeric Synechococcus PSI. The data were simulated based on the 2.5 Å structural model of PSI of Synechococcus elongatus using the Förster equation for energy transfer, and using the 0.6–1-ps charge-separation time and the value of 1.2–1.3 for the index of refraction that were obtained from the dynamics of a hypothetical PSI particle without red chls. The experimentally obtained lifetimes and spectra were reproduced well by assigning three of the chlorophyll-a (chla) dimers observed in the structure to the C708/C702RT pool of red chls present in PSI from both species. Essential for the simulation of the dynamics of Synechococcus PSI is the assignment of the single chla trimer in the structure to the C719/C708RT pool present in this species.

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