g-Anisotropy of the S2-state manganese cluster in single crystals of cyanobacterial photosystem II studied by W-band electron paramagnetic resonance spectroscopy.
The multiline signal from the S2-state manganese cluster in the oxygen evolving complex of photosystem II (PSII) was observed in single crystals of a thermophilic cyanobacterium Thermosynechococcus vulcanus for the first time by W-band (94 GHz) electron paramagnetic resonance (EPR). At W-band, spectra were characterized by the g-anisotropy, which enabled the precise determination of the tensor. Distinct hyperfine splittings (hfs's) as seen in frozen solutions of PSII at X-band (9.5 GHz) were detected in most of the crystal orientations relative to the magnetic field. In some orientations, however, the hfs's disappeared due to overlapping of a large number of EPR lines from eight crystallographic symmetry-related sites of the manganese cluster within the unit cell of the crystal. Analysis of the orientation-dependent spectral features yielded the following g-tensor components: g(x) = 1.988, g(y) = 1.981, g(z) = 1.965. The principal values suggested an approximate axial symmetry around the Mn(III) ion in the cluster.
Matsuoka
Hideto
H
Institute for Molecular Science, Okazaki 444-8585, Japan.
Furukawa
Ko
K
Kato
Tatsuhisa
T
Mino
Hiroyuki
H
Shen
Jian-Ren
JR
Kawamori
Asako
A
D003460:Crystallization; D000458:Cyanobacteria / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods*; D008345:Manganese / Q000737:chemistry*; D045332:Photosystem II Protein Complex / Q000737:chemistry*
D045332:Photosystem II Protein Complex; D008345:Manganese