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Structural Changes during ATP Hydrolysis Activity of the ATP Synthase from Escherichia coli as Revealed by Fluorescent Probes

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Abstract

F1F0-ATPase complexes undergo several changes in their tertiary and quaternary structureduring their functioning. As a possible way to detect some of these different conformationsduring their activity, an environment-sensitive fluorescence probe was bound to cysteineresidues, introduced by site-directed mutagenesis, in the γ subunit of the Escherichia colienzyme. Fluorescence changes and ATP hydrolysis rates were compared under variousconditions in F1 and in reconstituted F1F0. The results are discussed in terms of possible modes ofoperation of the ATP synthases.

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  1. Laboratory of Biochemistry and Biophysics, Department of Biology, University of Bologna, Via Irnerio 42, I-40126, Bologna, Italy

    Paola Turina

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  1. Paola Turina
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Turina, P. Structural Changes during ATP Hydrolysis Activity of the ATP Synthase from Escherichia coli as Revealed by Fluorescent Probes . J Bioenerg Biomembr 32, 373–381 (2000). https://doi.org/10.1023/A:1005528003709

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