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   <subfield code="a">Photoinhibition and repair in Dunaliella salina acclimated to different growth irradiances</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Irene Baroli, Anastasios Melis]</subfield>
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   <subfield code="a">The light-dependent rate of photosystem-II (PSII) damage and repair was measured in photoautotrophic cultures of Dunaliella salina Teod. grown at different irradiances in the range 50-3000 μmol photons · m−2· s−1. Rates of cell growth increased in the range of 50-800 μmol photons·m−2·s−1, remained constant at a maximum in the range of 800-1,500 μmol photons·m−2 ·s−1, and declined due to photoinhibition in the range of 1500-3000 μmol photons·m−2·s−1. Western blot analyses, upon addition of lincomycin to the cultures, revealed first-order kinetics for the loss of the PSII reaction-center protein (D1) from the 32-kDa position, occurring as a result of photodamage. The rate constant of this 32-kDa protein loss was a linear function of cell growth irradiance. In the presence of lincomycin, loss of the other PSII reaction-center protein (D2) from the 34-kDa position was also observed, occurring with kinetics similar to those of the 32-kDa form of D1. Increasing rates of photodamage as a function of irradiance were accompanied by an increase in the steady-state level of a higher-molecular-weight protein complex (≈ 160-kDa) that cross-reacted with D1 antibodies. The steady-state level of the 160-kDa complex in thylakoids was also a linear function of cell growth irradiance. These observations suggest that photodamage to D1 converts stoichiometric amounts of D1 and D2 (i.e., the D1/D2 heterodimer) into a ≈160-kDa complex. This complex may help to stabilize the reaction-center proteins until degradation and replacement of D1 can occur. The results indicated an intrinsic half-time of about 60 min for the repair of individual PSII units, supporting the idea that degradation of D1 after photodamage is the rate-limiting step in the PSII repair process.</subfield>
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   <subfield code="a">Springer-Verlag, 1996</subfield>
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  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">D1 protein</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">Dunaliella</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">Green algae</subfield>
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   <subfield code="a">Photodamage</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">Photoinhibition</subfield>
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   <subfield code="a">Photosystem II</subfield>
   <subfield code="2">nationallicence</subfield>
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  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">Chl : chlorophyll</subfield>
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   <subfield code="a">PSI : photosystem I</subfield>
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   <subfield code="a">PSII : photosystem II</subfield>
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   <subfield code="a">D1 : the 32-kDa reaction-center protein of PSII, encoded by the chloroplast psbA gene</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">D2 : the 34-kDa reactioncenter protein of PSII, encoded by the chloroplast psbD gene</subfield>
   <subfield code="2">nationallicence</subfield>
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  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">QA : primary electron-accepting plastoquinone of PSII</subfield>
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   <subfield code="a">Baroli</subfield>
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   <subfield code="u">Department of Plant Biology, University of California, 411 Koshland Hall, 94720-3102, Berkeley, CA, USA</subfield>
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