Change search
ReferencesLink to record
Permanent link

Direct link
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 1520-4995, E-ISSN 0006-2960, 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.
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:su:diva-108369DOI: 10.1021/bi5009672ISI: 000341801000001OAI: diva2:758174


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

Open Access in DiVA

No full text

Other links

Publisher's full text

Search in DiVA

By author/editor
Sjöholm, Johannes
By organisation
Department of Biochemistry and Biophysics
In the same journal
Biochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 22 hits
ReferencesLink to record
Permanent link

Direct link