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Spectroscopic Evidence for a Redox-Controlled Proton Gate at Tyrosine D in Photosystem II
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Molecular Biomimetics.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Molecular Biomimetics.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Molecular Biomimetics.
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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Chemical Sciences
Identifiers
URN: urn:nbn:se:uu:diva-235168DOI: 10.1021/bi5009672ISI: 000341801000001PubMedID: 25180978OAI: oai:DiVA.org:uu-235168DiVA: diva2:761259
Available from: 2014-11-06 Created: 2014-10-29 Last updated: 2017-12-05Bibliographically approved

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Sjöholm, JohannesMamedov, FikretStyring, Stenbjörn

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