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The chloroplast ATP synthase: Structural changes during catalysis

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Abstract

This article summarizes some of the evidence for the existence of light-driven structural changes in theε andγ subunits of the chlorplast ATP synthase. Formation of a transmembrane proton gradient results in: (1) a change in the position of theε subunit such that it becomes exposed to polyclonal antibodies and to reagents which selectively modifyεLys109; (2) enhanced solvent accessibility of several sulfhydryl residues on theγ subunit; and (3) release/ exchange of tightly bound ADP from the enzyme. These and related experimental observations can, at least partially, be explained in terms of two different bound conformational states of theε 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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  1. Department of Biochemistry, The University of Kansas, 66045, Lawrence, Kansas

    Mark L. Richter & Fei Gao

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  1. Mark L. Richter
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  2. Fei Gao
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Richter, M.L., Gao, F. The chloroplast ATP synthase: Structural changes during catalysis. J Bioenerg Biomembr 28, 443–449 (1996). https://doi.org/10.1007/BF02113987

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  • DOI: https://doi.org/10.1007/BF02113987

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