Excited state equilibration in the photosystem I-light-harvesting I complex: P700 is almost isoenergetic with its antenna

Roberta Croce, Giuseppe Zucchelli, Flavio M. Garlaschi, Roberto Bassi, Robert C. Jennings*

*Corresponding author for this work

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

Photosystem I with its full antenna complement (PSI-LHCI) has been prepared by mild detergent solubilization with octyl β-D-glucopyranoside from maize thylakoids. A preliminary polypeptide analysis is presented. At room temperature, the steady-state fluorescence derives from an almost perfectly thermalized state, as demonstrated by a Stepanov analysis, in which about 90% of the excited states are associated with the red chlorophyll spectral forms absorbing above 700 nm. Equilibration is temperature-sensitive and is lost at T < 200 K. A careful analysis of fluorescence between 75 and 280 K clearly demonstrates the presence of at least three red chlorophyll spectral forms with emission maxima at 720, 730, and 742 nm, the absorption origin bands of which have been calculated at 714, 725, and 738 nm. On the basis of a minor deviation from thermal equilibration around 695 nm, it is suggested that at least 3-4 antenna chlorophylls, with an average absorption near 695 nm, are strongly coupled to P700. Thermodynamic analysis of absorption and fluorescence spectra indicates that the equilibrium, absorption-weighted excited state population of the P700 dimer is around 0.013 assuming that the low-energy exciton state possesses all the oscillator strength. The average free energy for excitation transfer from antenna to P700 is thus calculated to be -0.26 kT at room temperature. This indicates that P700 is almost isoenergetic with its antenna at room temperature when the red forms are taken fully into account. From the calculated excited state population of P700, we estimate that the primary charge separation rate in PSI is 1-2 ps-1.

Original languageEnglish
Pages (from-to)8572-8579
Number of pages8
JournalBiochemistry
Volume35
Issue number26
DOIs
Publication statusPublished - 1996

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