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Spectroscopic Evidence for a Redox-Controlled Proton Gate at Tyrosine D in Photosystem II
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
2014 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 53, no 36, 5721-5723 p.Article in journal (Refereed) Published
Abstract [en]

Tyrosine D (TyrD) is one of two well-studied redox active tyrosines in Photosystem II. TyrD shows redox kinetics much slower than that of its homologue, TyrZ, and is normally present as a stable deprotonated radical (TyrD<bold>). We have used time-resolved continuous wave electron paramagnetic resonance and electron spin echo envelope modulation spectroscopy to show that deuterium exchangeable protons can access TyrD on a time scale that is much faster (50</bold>100 times) than that previously observed. The time of H/D exchange is strongly dependent on the redox state of TyrD. This finding can be related to a change in position of a water molecule close to TyrD.

Place, publisher, year, edition, pages
2014. Vol. 53, no 36, 5721-5723 p.
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Biochemistry and Molecular Biology
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URN: urn:nbn:se:su:diva-108369DOI: 10.1021/bi5009672ISI: 000341801000001OAI: oai:DiVA.org:su-108369DiVA: diva2:758174
Note

AuthorCount:3;

Available from: 2014-10-24 Created: 2014-10-22 Last updated: 2017-12-05Bibliographically approved

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