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Updated: Jun 23, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
Picosecond time-resolved fluorescence from detergent-free photosystem I particles
Abstract:
Picosecond time-resolved fluorescence measurements have been taken on a detergent-free P700-enriched complex at room temperature isolated from the blue-green alga Phormidium luridum with a chlorophyll a to reaction center ratio of 100. Emission at greater than 665 nm is characterized by two exponential-decay components. A fast component, which dominates the initial decay with an average lifetime of 16 ps and 87% amplitude, is attributed to excitations in the core antenna chlorophyll-proteins, which are rapidly trapped by the primary electron donor, P700. A second component, with an average lifetime of 106 ps and 13% amplitude, is attributed to the peripheral antenna proteins. For 532-nm, 30-ps pulse excitation the results are virtually independent of fluence in the range of 2 x 10(12) to 4 x 10(16) photons/cm(2) and the oxidation state of P700. Addition of sodium dodecyl sulfate to 0.1% causes the second component's lifetime to increase by an average of a factor of 2.5. Only minor changes are observed in the first component's lifetime and the relative amplitudes of the two components. Two fractions isolated from the detergent-treated samples have also been examined. Our results indicate that excitation energy transfer within photosystem I is very efficient and that the excitation kinetics of the antennae may be limited by the trapping rate of P700 or strongly affected by the heterogeneity of the antennae.
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