Spectroscopic Evidence for a Redox-Controlled Proton Gate at Tyrosine D in Photosystem II
2014 (English)In: Biochemistry, ISSN 1520-4995, E-ISSN 0006-2960, Vol. 53, no 36, 5721-5723 p.Article in journal (Refereed) Published
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.
IdentifiersURN: urn:nbn:se:uu:diva-235168DOI: 10.1021/bi5009672ISI: 000341801000001PubMedID: 25180978OAI: oai:DiVA.org:uu-235168DiVA: diva2:761259