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Split Electron Paramagnetic Resonance signal induction in photosystem II suggests two binding sites in the S2 state for the substrate analogue methanol
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.
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2013 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 52, no 21, 3669-3677 p.Article in journal (Refereed) Published
Abstract [en]

Illuminating a photosystem II sample at low temperatures (here 5–10 K) yields so-called split signals detectable with continuous wave-electron paramagnetic resonance (CW-EPR). These signals reflect the oxidized, deprotonated radical of D1-Tyr161 (YZ) in a magnetic interaction with the CaMn4 cluster in a particular S state. The intensity of the split EPR signals are affected by the addition of the water substrate analogue methanol. This was previously shown by the induction of split EPR signals from the S1, S3, and S0 states [Su, J.-H. et al. (2006) Biochemistry 45, 7617–7627.]. Here, we use two split EPR signals induced from photosystem II trapped in the S2 state to further probe the binding of methanol in an S state dependent manner. The signals are induced with either visible or near-infrared light illumination provided at 5–10 K where methanol cannot bind or unbind from its site. The results imply that the binding of methanol not only changes the magnetic properties of the CaMn4 cluster but also the hydrogen bond network in the oxygen evolving complex (OEC), thereby affecting the relative charge of the S2 state. The induction mechanisms for the two split EPR signals are different resulting in two different redox states, S2YZ and S1YZ respectively. The two states show different methanol dependence for their induction. This indicates the existence of two binding sites for methanol in the CaMn4 cluster. It is proposed that methanol binds to MnA with high affinity and to MnD with lower affinity. The molecular nature and S-state dependence of the methanol binding to each respective site are discussed.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2013. Vol. 52, no 21, 3669-3677 p.
National Category
Biochemistry and Molecular Biology Biophysics
Research subject
Biochemistry
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URN: urn:nbn:se:uu:diva-203643DOI: 10.1021/bi400144eOAI: oai:DiVA.org:uu-203643DiVA: diva2:637181
Available from: 2013-07-16 Created: 2013-07-16 Last updated: 2017-12-06Bibliographically approved

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Sjöholm, JohannesHo, FelixMamedov, FikretStyring, Stenbjörn

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Molecular BiomimeticsDepartment of Chemistry - Ångström
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