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The protonation state around Tyr(D)/Tyr((D)) over dot in photosystem II is reflected in its biphasic oxidation kinetics
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Molecular Biomimetics. Stockholm Univ, Dept Biochem & Biophys, Arrhenius Labs Nat Sci, SE-10691 Stockholm, Sweden..
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. Imperial Coll London, Dept Life Sci, Sir Ernst Chain Bldg, London SW7 2AZ, England..
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2017 (English)In: Biochimica et Biophysica Acta - Bioenergetics, ISSN 0005-2728, E-ISSN 1879-2650, Vol. 1858, no 2, 147-155 p.Article in journal (Refereed) Published
Abstract [en]

The tyrosine residue D2-Tyr160 (Tyr(D)) in photosystem II (PSII) can be oxidized through charge equilibrium with the oxygen evolving complex in PSII. The kinetics of the electron transfer from Tyr(D) has been followed using time resolved EPR spectroscopy after triggering the oxidation of pre-reduced Tyr(D) by a short laser flash. After its oxidation Tyro is observed as a neutral radical (Tyr((D)) over dot) indicating that the oxidation is coupled to a deprotonation event. The redox state of Tyro was reported to be determined by the two water positions identified in the crystal structure of PSII [Saito et al. (2013) Proc. Natl. Acad. Sci. USA 110, 7690]. To assess the mechanism of the proton coupled electron transfer of Tyr(D) the oxidation kinetics has been followed in the presence of deuterated buffers, thereby resolving the kinetic isotope effect (KIE) of Tyro oxidation at different H/D concentrations. Two kinetic phases of Tyro oxidation - the fast phase (msec-sec time range) and the slow phase (tens of seconds time range) were resolved as was previously reported [Vass and Styring (1991) Biochemistry 30, 830]. In the presence of deuterated buffers the kinetics was significantly slower compared to normal buffers. Furthermore, although the kinetics were faster at both high pH and pD values the observed KIE was found to be similar (similar to 2.4) over the whole pL range investigated. We assign the fast and slow oxidation phases to two populations of PSII centers with different water positions, proximal and distal respectively, and discuss possible deprotonation events in the vicinity of Tyro.

Place, publisher, year, edition, pages
2017. Vol. 1858, no 2, 147-155 p.
Keyword [en]
Photosystem II, Tyrosine D, Electron transfer, Proton transfer, Deuterium isotope effect
National Category
Biochemistry and Molecular Biology Biophysics
Identifiers
URN: urn:nbn:se:uu:diva-316938DOI: 10.1016/j.bbabio.2016.11.002ISI: 000392776400007PubMedID: 27823941OAI: oai:DiVA.org:uu-316938DiVA: diva2:1079647
Funder
Swedish Research Council, 621-2013-5937Swedish Energy Agency, 11674-5Knut and Alice Wallenberg Foundation, KAW 2011.0067
Available from: 2017-03-09 Created: 2017-03-09 Last updated: 2017-03-09Bibliographically approved

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Sjöholm, JohannesHo, FelixAhmadova, NigarHammarström, LeifMamedov, FikretStyring, Stenbjörn
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