Jun 14, 2006

Split EPR signals from photosystem II are modified by methanol, reflecting S state-dependent binding and alterations in the magnetic coupling in the CaMn4 cluster

Biochemistry
Ji-Hu SuStenbjörn Styring

Abstract

Methanol binds to the CaMn4 cluster in photosystem II (PSII). Here we report the methanol dependence of the split EPR signals originating from the magnetic interaction between the CaMn4 cluster and the Y(Z)* radical in PSII which are induced by illumination at 5 K. We found that the magnitudes of the "split S1" and "split S3" signals induced in the S1 and S3 states of PSII centers, respectively, are diminished with an increase in the methanol concentration. The methanol concentrations at which half of the respective spectral changes had occurred ([MeOH](1/2)) were 0.12 and 0.57%, respectively. By contrast, the "split S0" signal induced in the S0 state is broadened, and its amplitude is enhanced. [MeOH](1/2) for this change was found to be 0.54%. We discuss these observations with respect to the location and nature of the methanol binding site. Furthermore, by comparing this behavior with methanol effects reported for other EPR signals in the different S states, we propose that the observed methanol-dependent changes in the split S1 and split S0 EPR signals are caused by an increase in the extent of magnetic coupling within the cluster.

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Mentioned in this Paper

Sodium Methoxide
Plasma Protein Binding Capacity
Etiology
Ligand Binding Domain
Binding (Molecular Function)
Photosynthetic Reaction Center Complex Proteins
Illumination Technique
Illumination (Procedure)
Methanol
Dose-Response Relationship, Drug

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