The Use of Several Energy‐Coupling Reactions in Characterizing Mutants of Escherichia coli K12 Defective in Oxidative Phosphorylation

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Abstract
Oxidative phosphorylation, ATP-32Pi exchange, ATP-dependent quenching of acridine-dye fluorescence, ATP-dependent transhydrogenase and ATP-dependent transport of thiomethyl .beta.-D-galactoside are shown to be experimentally equivalent tools to study the functional state of the ATPase complex in E. coli wild-type and mutant strains defective in oxidative phosphorylation. Ten mutants in the ATPase complex were classified having lesions in the unc A,B region of the chromosome. The 1st mutant type lacks ATPase activity, but the membrane integrated part of the complex remains functional (class I). The 2nd mutant type lacks a functional membrane-integrated part, but retains ATPase activity (class II). The 3rd mutant type is defective in both parts of the ATPase complex (class III).

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