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Precise location of the Cu(II)-inhibitory binding site in higher plant and bacterial photosynthetic reaction centers as probed by light-induced absorption changes

AutorYruela Guerrero, Inmaculada ; Alfonso Lozano, Miguel ; Ortiz de Zarate Avila, Iñaki; Montoya Blanco, Guillermo ; Picorel Castaño, Rafael
Fecha de publicación1993
EditorAmerican Society for Biochemistry and Molecular Biology
CitaciónJournal of Biological Chemistry 268: 1684-1689 (1993)
ResumenLight-dependent absorption change at 325 nm, ascribed to Q(A) activity, was strongly reduced in the presence of Cu(II) in oxygen-evolving core complex. This change was much less affected in the presence of the herbicide 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU), indicating that the Cu(II)- binding site is different from that of the DCMU and that Cu(II) blocks Q(A) reduction. Cu(II) did not eliminate the absorption change at 545 nm, ascribed to pheophytin reduction, in Na2S2O4-treated oxygen-evolving core and D1- D2-cytochrome b559 complexes. This indicates that Cu(II) does not affect the electron transport between P680 and pheophytin. Moreover, the activity of the bacterial reaction center probed by the absorption change at 790 nm was inhibited by Cu(II), but the signal at 530 nm, associated to the reduction of bacteriopheophytin in Na2S2O4-treated reaction center, was not inhibited. We conclude that Cu(II) impaired the photosynthetic electron transport between pheophytin and Q(A) in both higher plants and photosynthetic bacteria. Cu(II) would bind to an amino acid(s) highly conserved in non- oxygenic and oxygenic reaction centers, which is(are) necessary for the electron transfer between pheophytin and Q(A). Based on the atomic structure of the bacterial reaction center several schemes of possible Cu(II) binding are shown.
URIhttp://hdl.handle.net/10261/121137
DOInull
Identificadoresdoi: null
issn: 0021-9258
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