ISSN:
1573-6881
Keywords:
ATP synthase
;
E. coli
;
fluorescence
;
conformational changes
;
membrane energization
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Physics
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1005528003709
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