PMID: 8951092Oct 1, 1996Paper

The chloroplast ATP synthase: structural changes during catalysis

Journal of Bioenergetics and Biomembranes
M L Richter, F Gao

Abstract

This article summarizes some of the evidence for the existence of light-driven structural changes in the epsilon and gamma subunits of the chloroplast ATP synthase. Formation of a transmembrane proton gradient results in: (1) a changed in the position of the epsilon subunit such that it becomes exposed to polyclonal antibodies and to reagents which selectively modify epsilon Lys109; (2) enhanced solvent accessibility of several sulfhydryl residues on the gamma subunit; and (3) release/exchange of tightly bound ADP from the enzyme. Theses and related experimental observations can, at least partially, be explained in terms of two different bound conformational states of the epsilon subunit. Evidence for structural changes in the enzyme which are driven by light or nucleotide binding is discussed with special reference to the popular rotational model for catalysis.

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Citations

Aug 30, 2008·Science in China. Series C, Life Sciences·X ShiY Shen
May 13, 2006·Journal of Bioenergetics and Biomembranes·Mark L RichterKrzysztof K Kuczera
Mar 12, 2004·Annual Review of Plant Physiology and Plant Molecular Biology·R. E. McCartyE. A. Johnson
Jul 20, 1999·Annual Review of Biophysics and Biomolecular Structure·R K NakamotoM K al-Shawi
May 17, 2006·Biochimica Et Biophysica Acta·Boris A FenioukMasasuke Yoshida
Apr 1, 2006·Memory·George P StuartNavi Bhagrath
Jun 6, 2000·Biochimica Et Biophysica Acta·M L RichterB Huchzermeyer

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