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  • Ahmadova, NigarUppsala universitet,Molekylär biomimetik (author)

Formation of tyrosine radicals in photosystem II under far-red illumination

  • Article/chapterEnglish2018

Publisher, publication year, extent ...

  • 2017-09-18
  • Springer Science and Business Media LLC,2018
  • electronicrdacarrier

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  • LIBRIS-ID:oai:DiVA.org:uu-320914
  • https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-320914URI
  • https://doi.org/10.1007/s11120-017-0442-3DOI

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  • Language:English
  • Summary in:English

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  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

Notes

  • Photosystem II (PS II) contains two redox-active tyrosine residues on the donor side at symmetrical positions to the primary donor, P680. TyrZ, part of the water-oxidizing complex, is a preferential fast electron donor while TyrD is a slow auxiliary donor to P680 +. We used PS II membranes from spinach which were depleted of the water oxidation complex (Mn-depleted PS II) to study electron donation from both tyrosines by time-resolved EPR spectroscopy under visible and far-red continuous light and laser flash illumination. Our results show that under both illumination regimes, oxidation of TyrD occurs via equilibrium with TyrZ • at pH 4.7 and 6.3. At pH 8.5 direct TyrD oxidation by P680 + occurs in the majority of the PS II centers. Under continuous far-red light illumination these reactions were less effective but still possible. Different photochemical steps were considered to explain the far-red light-induced electron donation from tyrosines and localization of the primary electron hole (P680 +) on the ChlD1 in Mn-depleted PS II after the far-red light-induced charge separation at room temperature is suggested.

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  • Mamedov, Fikret,Ph.D., Dr.Sci.Uppsala universitet,Molekylär biomimetik(Swepub:uu)fimam179 (author)
  • Uppsala universitetMolekylär biomimetik (creator_code:org_t)

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  • In:Photosynthesis Research: Springer Science and Business Media LLC136:1, s. 93-1060166-85951573-5079

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