Apr 27, 1999

The role of cytochrome b559 and tyrosineD in protection against photoinhibition during in vivo photoactivation of photosystem II

Biochimica Et Biophysica Acta
A MagnusonStenbjörn Styring

Abstract

In vivo photoactivation of Photosystem II was studied in the FUD39 mutant strain of the green alga Chlamydomonas reinhardtii which lacks the 23 kDa protein subunit involved in water oxidation. Dark grown cells, devoid of oxygen evolution, were illuminated at 0.8 μE m-2s-1 light intensity which promotes optimal activation of oxygen evolution, or at 17 μE m-2s-1, where photoactivation compete with deleterious photodamage. The involvement of the two redox active cofactors tyrosineD and cytochrome b559 during the photoactivation process, was investigated by EPR spectroscopy. TyrosineD on the D2 reaction center protein functions as auxiliary electron donor to the primary donor P+680 during the first minutes of photoactivation at 0.8 μE m-2s-1 (compare with Rova et al., Biochemistry, 37 (1998) 11039-11045.). Here we show that also cytochrome b559 was rapidly oxidized during the first 10 min of photoactivation with a similar rate to tyrosineD. This implies that both cytochrome b559 and tyrosineD may function as auxiliary electron donors to P+680 and/or the oxidized tyrosine&z.ccirf;Z on the D1 protein, to avoid photoinhibition before successful photoactivation was accomplished. As the catalytic water-oxidation successively became acti...Continue Reading

  • References18
  • Citations22

References

  • References18
  • Citations22

Citations

Mentioned in this Paper

AT 17
Oxidation
Photoinhibition
Mutant
Reaction Center
Electron Spin Resonance Spectroscopy
Oxidation-Reduction
Cytochrome b559
Tyrosine Measurement
Chemical cofactor

About this Paper

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