Specific isotopic labeling and photooxidation-linked structural changes in the manganese -stabilizing subunit of photosystem II

doi:10.1074/jbc.M307148200

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Papers In Press, published online ahead of print August 25, 2003
J. Biol. Chem, 10.1074/jbc.M307148200
Submitted on July 3, 2003
Revised on August 19, 2003
Accepted on August 25, 2003

Specific isotopic labeling and photooxidation-linked structural changes in the manganese -stabilizing subunit of photosystem II

Roseann K. Sachs, Kelly M. Halverson, and Bridgette A. Barry

Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, St. Paul, MN 55108

Corresponding Author: barry{at}biosci.cbs.umn.edu

Photosystem II (PSII), oxidizes water to molecular oxygen; the catalytic site is a cluster of four manganese ions. The catalytic site undergoes four sequential light-driven oxidation steps to form oxygen; these sequentially oxidized states are referred to as the Sn states, where n refers to the number of oxidizing equivalents stored. The extrinsic manganese stabilizing protein (MSP) of PSII influences the efficiency and stability of the manganese cluster, as well as the rates of the S state transitions. To understand how MSP influences photosynthetic water oxidation, we have employed isotope-editing and difference FT-IR spectroscopy. MSP was expressed in E. coli under conditions in which MSP aspartic and glutamic acid residues label at yields of 65% a nd 41%, respectively. Asparagine and glutamine were also labeled by this approach. GC/MS analysis was consistent with little scrambling of label into other amino acid residues and with no significant scrambling into the peptide bond. Selectively labeled MSP was then reconstituted to PSII, which had been stripped of native MSP. Difference FT-IR spectroscopy was used to probe the S1QA to S2QA- transition at 200 K, as well as the S1QB to S2QB- transition at 277 K. These experiments show that aspargine, glutamine, and glutamate residues in MSP are perturbed by photooxidation of Mn during the S1 to S2 transition. b

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