Oxidative phosphorylation by mutant Escherichia coli membranes with impaired proton permeability.

G. B. Cox, D. A. Jans, F. Gibson, L. Langman, A. E. Senior, A. L. Fimmel

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Abstract

The effect on the function of the Escherichia coli F1F0-ATPase of the substitution of leucine-31 by phenylalanine in the c-subunit of the enzyme was examined. The assembly of the mutant c-subunit requires an increased gene dosage [Jans, Fimmel, Langman, James, Downie, Senior, Ash, Gibson & Cox (1983) Biochem. J. 211, 717-726], and this was achieved by incorporation of the uncE408 or uncE463 alleles on to F-plasmids or multicopy plasmids. Membranes from strains carrying either the uncE463 or uncE408 alleles on F-plasmids or multicopy plasmids were capable of carrying out oxidative phosphorylation. In particular, membranes from strain AN1928 (pAN162, uncE463) gave phosphorylation rates and P/O ratios equal to or greater than those obtained for the control strain AN1460 (pAN45, unc+). However, the mutant membranes, on removal of the F1-ATPase, appeared to be proton-impermeable. The ATPase activity of the mutant membranes was also resistant to the inhibitor dicyclohexylcarbodi-imide.

Original languageEnglish
Pages (from-to)143-150
Number of pages8
JournalBiochemical Journal
Volume216
Issue number1
DOIs
Publication statusPublished - 1 Jan 1983
Externally publishedYes

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