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The redox potential of the primary quinone Q A of bacterial photosynthesis is independent of the divalent metal ion
Author(s) -
Buchanan Susan K.,
Dismukes G.Charles,
Prince Roger C.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80788-9
Subject(s) - divalent , chemistry , redox , histidine , ferrous , photosynthetic reaction centre , quinone , covalent bond , inorganic chemistry , metal , electron transfer , ion , metal ions in aqueous solution , manganese , photochemistry , stereochemistry , biochemistry , organic chemistry , enzyme
The function of the ferrous ion which links the primary and secondary quinone electron acceptors, Q A and Q B , via histidine ligands from the reaction center protein of the photosynthetic bacterium Rbodobacter sphaeroids (Y) has been investigated by substitution with Mn(II), Cu(II) and Zn(II), using biosynthetic incorporation of the metal ion. The midpoint potential and pH dependence for reduction of Q A in chromatophore membranes were found to be indistinguishable for all four divalent ions, and in agreement with earlier results on the R26 and Ga strains of R. sphaeroides containing only iron. We therefore conclude that the divalent ion contributes no functionally significant covalent coupling to the primary acceptor and that these metals have no differential electrostatic influence. Furthermore, inhibition of photoreduction of Q B by the herbicide ametryne was found to be the same for all four samples. Thus, these four divalent ions exhibit no differential influence on the binding properties of this herbicide in the Q B site.