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Title:The Effects of Chemical Modification Upon Herbicide Binding in Thylakoid Membranes of Spinacia Oleracea (Spinach) and Amaranthus Hybridus (Pigweed), and The Photochemical Reaction Center of Rhodobacter Sphaeroides R26
Author(s):Paterson, David Ross
Department / Program:Plant Biology
Discipline:Plant Biology
Degree Granting Institution:University of Illinois at Urbana-Champaign
Subject(s):Agriculture, Plant Culture
Abstract:Dicyclohexylcarbodiimide inhibits electron transfer between Q$\sb{\rm A}$ and Q$\sb{\rm B}$ in both higher plants and photosynthetic bacteria in an analogous manner to that seen for the classic Photosystem II inhibitors such as diuron and atrazine. It does not bind to the same binding domain as these inhibitors. It does not bind covalently, suggesting that the mechanism of inhibition in this system is a novel one for this protein modification reagent.
Amaranthus hybridus shows a heterogeneous population of diuron binding sites. Two populations are readily observed in the absence of ferricyanide. This heterogeneity of binding sites is also seen in spinach, but in the presence of ferricyanide.
The structural integrity of Photosystem II plays a crucial role in diuron binding. When the membrane structure is altered by detergent treatment, removal of divalent cations, or phosphorylation, the binding affinity of diuron is increased.
Azido-diuron binds to two polypeptides in thylakoid membranes. A 32 kD polypeptide which is probably the so-called herbicide binding protein. The other polypeptide has an apparent molecular weight of 50 kD. The identity of the polypeptide is unknown.
Models for predicting secondary structure were used to examine the herbicide binding domain, and found to be unsuitable for predicting secondary structure in integral membrane proteins.
Issue Date:1987
Description:282 p.
Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1987.
Other Identifier(s):(UMI)AAI8721732
Date Available in IDEALS:2014-12-16
Date Deposited:1987

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