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Photosystem II single crystals studied by EPR spectroscopy at 94 GHz: the tyrosine radical Y(D)(*).
Hofbauer, W; Zouni, A; Bittl, R; Kern, J; Orth, P; Lendzian, F; Fromme, P; Witt, H T; Lubitz, W.
Afiliação
  • Hofbauer W; Max-Volmer-Institut für Biophysikalische Chemie und Biochemie, Technische Universität Berlin, Strasse des 17, Juni 135, D-10623 Berlin, Germany.
Proc Natl Acad Sci U S A ; 98(12): 6623-8, 2001 Jun 05.
Article em En | MEDLINE | ID: mdl-11381107
ABSTRACT
Electron paramagnetic resonance (EPR) spectroscopy at 94 GHz is used to study the dark-stable tyrosine radical Y(D)(*) in single crystals of photosystem II core complexes (cc) isolated from the thermophilic cyanobacterium Synechococcus elongatus. These complexes contain at least 17 subunits, including the water-oxidizing complex (WOC), and 32 chlorophyll a molecules/PS II; they are active in light-induced electron transfer and water oxidation. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with four PS II dimers per unit cell. High-frequency EPR is used for enhancing the sensitivity of experiments performed on small single crystals as well as for increasing the spectral resolution of the g tensor components and of the different crystal sites. Magnitude and orientation of the g tensor of Y(D)(*) and related information on several proton hyperfine tensors are deduced from analysis of angular-dependent EPR spectra. The precise orientation of tyrosine Y(D)(*) in PS II is obtained as a first step in the EPR characterization of paramagnetic species in these single crystals.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Complexo de Proteínas do Centro de Reação Fotossintética Idioma: En Revista: Proc Natl Acad Sci U S A Ano de publicação: 2001 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Complexo de Proteínas do Centro de Reação Fotossintética Idioma: En Revista: Proc Natl Acad Sci U S A Ano de publicação: 2001 Tipo de documento: Article