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Related Experiment Videos

Calcium exchange and structural changes during the photosynthetic oxygen evolving cycle.

Antonio De Riso1, David L Jenson, Bridgette A Barry

  • 1School of Chemistry and Biochemistry and the Petit Institute for Bioscience and Bioengineering, Georgia Institute of Technology, Atlanta, Georgia, USA.

Biophysical Journal
|June 20, 2006
PubMed
Summary

Strontium substitution in Photosystem II (PSII) reveals its role in the oxygen-evolving complex. This study shows how strontium affects the calcium site and hydrogen bonding during the catalytic cycle.

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Area of Science:

  • Biochemistry
  • Photosynthesis Research
  • Structural Biology

Background:

  • Photosystem II (PSII) is crucial for oxygenic photosynthesis, catalyzing water oxidation and plastoquinone reduction.
  • The oxygen-evolving complex (OEC) within PSII, containing Mn, Ca, and Cl, is essential for oxygen production through sequential photooxidation reactions.
  • Calcium is vital for oxygen production, with strontium being the only known divalent cation to substitute for calcium while maintaining activity.

Purpose of the Study:

  • To investigate the effects of strontium substitution for calcium on the oxygen-evolving complex of Photosystem II.
  • To elucidate the role of the calcium site and associated hydrogen bonding network during the catalytic S-state cycle.
  • To propose a modified S-state model based on reaction-induced FT-IR studies of strontium-substituted PSII.

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Main Methods:

  • Utilized reaction-induced Fourier Transform Infrared (FT-IR) spectroscopy on hydrated Photosystem II preparations.
  • Studied the full S-state cycle, including transitions from S1' to S2' and S3' to S0' to S1'.
  • Analyzed difference FT-IR spectra to identify photoinduced conformational changes and probe the calcium site and hydrogen bonding network.

Main Results:

  • Observed long-lived photoinduced conformational changes in the oxygen-evolving complex upon strontium substitution.
  • Identified vibrational bands sensitive to calcium site substitutions, indicating perturbations during the S1' to S2' transition.
  • Found evidence of hydrogen bonding network perturbation involving calcium, water, and peptide carbonyls during S3' to S0' and S0' to S1' transitions.

Conclusions:

  • Strontium substitution for calcium in PSII leads to persistent shifts in divalent cation coordination.
  • The calcium site and its associated hydrogen bonding network are dynamically involved in the S-state cycle transitions.
  • A modified S-state model is proposed to account for the observed FT-IR data and literature findings on strontium-substituted PSII.