Oxidation‐Reduction Physical Chemistry of the Acceptor Quinone Complex in Bacterial Photosynthetic Reaction Centers: Evidence for a New Model of Herbicide Activity

作者: C. A. Wraight

DOI: 10.1002/IJCH.198100063

关键词:

摘要: The oxidation-reduction midpoint potential (Em) of the primary quinone (QA) acceptor complex bacterial photosynthetic reaction centers has been measured as a function pH in presence and absence ubiquinone o-phenanthroline (o-Phen). Reaction centers, isolated from Rhodopseudomonas sphaeroides, were incorporated into egg phosphatidylcholine vesicles. Contrary to earlier reports, Em was found exhibit pH-dependence very similar that observed chromatophores, with slope - 60 mV/pH up p K for Q−A/Q−A(H+) at 9.5–10.0. In reconstitute secondary (QB), Em/pH curve QA shifted lower potentials, indicating binding Qn (actually QBH2) suppressed by reduction QA. o-Phen, an inhibitor electron transport QB, raised pK and, pH-values below but not above this pK, reversed effects QB. o-Phen lowered had no effect it. These results are discussed terms interactions between sites QB (A- B-sites). It is suggested compete B-site mutually exclusive fashion, their relative strengths modulated redox protonation state preparations low content, inhibits photochemistry suggesting it can also A-site. Competitive displacement other inhibitors mode action broad class herbicides active Photosystem II plants. affinities various states concluded order strength is: Q−B → QBH2. This accounts atypical stability semiquinone average quinol, compared free pool. may be significant functioning quinones communicating reducing equivalents center complexes intact membrane.

参考文章(27)
Roger C. Prince, P.Leslie Dutton, The primary acceptor of bacterial photosynthesis: Its operating midpoint potential? Archives of Biochemistry and Biophysics. ,vol. 172, pp. 329- 334 ,(1976) , 10.1016/0003-9861(76)90084-9
Vittorio Moret, Silvano Pinamonti, Elena Fornasari, Polarographic study on the redox potential of ubiquinones Biochimica et Biophysica Acta. ,vol. 54, pp. 381- 383 ,(1961) , 10.1016/0006-3002(61)90388-2
W.F. Butler, D.C. Johnston, H.B. Shore, D.R. Fredkin, M.Y. Okamura, G. Feher, The electronic structure of Fe2+ in reaction centers from Rhodopseudomonas sphaeroides. I. Static magnetization measurements Biophysical Journal. ,vol. 32, pp. 967- 992 ,(1980) , 10.1016/S0006-3495(80)85030-2
Yadviga D. Halsey, William W. Parson, Identification of ubiquinone as the secondary electron acceptor in the photosynthetic apparatus of Chromatium vinosum. Biochimica et Biophysica Acta. ,vol. 347, pp. 404- 416 ,(1974) , 10.1016/0005-2728(74)90079-6
A. Vermeglio, T. Martinet, R. K. Clayton, Mode of inhibition of electron transport by orthophenanthroline in chromatophores and reaction centers of Rhodopseudomonas sphaeroides. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 77, pp. 1809- 1813 ,(1980) , 10.1073/PNAS.77.4.1809
R. A. Morton, U. Gloor, O. Schindler, G. M. Wilson, L. H. Chopard-dit-Jean, F. W. Hemming, O. Isler, W. M. F. Leat, J. F. Pennock, R. Rüegg, U. Schwieter, O. Wiss, Die Struktur des Ubichinons aus Schweineherzen Helvetica Chimica Acta. ,vol. 41, pp. 2343- 2357 ,(1958) , 10.1002/HLCA.19580410745