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Location of the extrinsic subunit PsbP in photosystem II studied by pulsed electron-electron double resonance
Authors:Mizue Asada  Taishi Nishimura  Kentaro Ifuku  Hiroyuki Mino
Affiliation:1. Division of Material Science (Physics), Graduate school of Science, Nagoya University, Furo-cho, Chikusa, Nagoya 464-8602, Japan;2. Graduate School of Biostudies, Kyoto University, Sakyo-ku, Kyoto 606–8502, Japan
Abstract:
The binding site of the extrinsic protein PsbP in plant photosystem II was mapped by pulsed electron-electron double resonance, using mutant spinach PsbP (Pro20Cys, Ser82Cys, Ala111Cys, and Ala186Cys) labeled with 4-maleimido-TEMPO (MSL) spin label. The distances between the spin label and the Tyr160 neutral radical (YD/>) in PsbD, the D2 subunit of plant photosystem II, were 50.8?±?3.5?Å, 54.9?±?4.0?Å, 57.8?±?4.9?Å, and 58.4?±?14.1?Å, respectively. The geometry inferred from these distances was fitted to the PsbP crystal structure (PDB: <a href=4RTI) to obtain the coordinates of YD/> relative to PsbP. These coordinates were then fitted under boundary conditions to the structure of cyanobacterial photosystem II (PDB: <a href=4UB6), by rotating on Euler angles centered at fixed YD/> coordinates. The result proposed two models which show possible acidic amino acid residues in CP43, CP47 and D2 that can bind the basic amino acids Arg48, Lys143, and Lys160 in PsbP.</td>
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Keywords:EPR  electron paramagnetic resonance  PELDOR  pulsed electron-electron double resonance  ESE  electron spin echo  CW  continuous wave  MW  microwave  Mes  2-morpholinoethasulfonic acid  PS II  photosystem II  OEC  oxygen-evolving complex  D  Tyr161 for higher plants (Tyr160 for cyanobacteria) of the D2 subunit in PS II  MSL  4-maleimido-TEMPO  TEMPO  2,2,6,6-tetramethylpiperidine 1-oxyl  EM  electron microscopy  Photosystem II  Extrinsic subunit  PsbP  EPR  PELDOR
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