The functional sites of chlorophylls in D1 and D2 subunits of Photosystem II identified by pulsed EPR

Photosynthesis Research - Tập 84 - Trang 187-192 - 2005
A. Kawamori1, T-A. Ono2, A. Ishii2, S. Nakazawa2, H. Hara3, T. Tomo4, J. Minagawa5, R. Bittl6, S.A. Dzuba7
1School of Science and Technology, Kwansei Gakuin University, Sanda, Japan
2The Institute of Physical and Chemical Research (RIKEN), Photodynamics Research Center, Sendai, Japan
3Division of EPR Application, Bruker Biospin, KK., Tsukuba, Japan
4Department of Physics, College of Humanities and Sciences, Nihon University, Tokyo, Japan
5Low Temperature Research Institute, Hokkaido University, Sapporo, Japan
6Institute of Experimental Physics, Free University of Berlin, Berlin, Germany
7Institute of Chemical Kinetics and Combustion, Russian Academy of Sciences, Novosibirsk, Russia

Tóm tắt

The functional site of ChlZ, an auxiliary electron donor to P680+, was determined by pulsed ELDOR applied to a radical pair of Y D • and Chlz+ in oriented PS II membranes from spinach. The radical-radical distance was determined to be 29.5 Å and its direction was 50° from the membrane normal, indicating that a chlorophyll on the D2 protein is responsible for the EPR Chlz+ signal. Spin polarized ESEEM (Electronin Spin Echo Envelop Modulation) of a 3Chl and Q A − radical pair induced by a laser flash was observed in reaction center D1D2Cytb559 complex, in which QA was functionally reconstituted with DBMIB and reduced chemically. Q A − ESEEM showed a characteristic oscillating time profile due to dipolar coupling with 3Chl. By fitting with the dipolar interaction parameters, the distance between 3Chl and Q A − was determined to be 25.9 Å, indicating that the accessory chlorophyll on the D1 protein is responsible for the 3Chl signal.

Tài liệu tham khảo

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