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Volume 270, Number 14, Issue of April 7, 1995 pp. 7896-7901
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Detection by Site-specific Disulfide Cross-linking of a Conformational Change in Binding of Escherichia coli Pyruvate Oxidase to Lipid Bilayers

(Received for publication, January 10, 1995)

Ying-Ying Chang ,  John E. Cronan Jr.

Escherichia coli pyruvate oxidase, a peripheral membrane homotetrameric flavoprotein, exposes its C-terminal lipid binding site in the presence of substrate pyruvate and co-factor thiamine pyrophosphate Mg and binds tightly to phospholipid bilayers during catalysis. Using site-specific disulfide cross-linking, we demonstrate that disulfide cross-links are formed between C termini of D560C pyruvate oxidase and that the degree of cross-linking is greatly increased by the presence of substrate and co-factors indicating a conformational change that results in juxtaposition of two subunit C termini. The cross-linked oxidase is enzymatically active and remains able to associate with lipid micelles. These results argue strongly that lipid bilayer binding of pyruvate oxidase involves pairing of the C termini of two subunits.



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Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.