Oxidative phosphorylation in mutants of Escherichia coli defective in energy transduction

D. L. Gutnick*, B. I. Kanner, P. W. Postma

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Two mutants defective in oxidative phosphorylation have been isolated from Escherichia coli K12. The mutants lack ATP-driven transhydrogenase activity and exhibit P/NADH ratios, as measured in whole cells, of 0.04 and 0.16, respectively, as compared with a parental value of 2.1. Respiration-linked transhydrogenase was detected in membrane particles from the two strains. One of the mutants was defective in membrane (Mg2+-Ca2+-ATPase activity while the second strain exhibited a level of ATPase activity comparable to that in the parent. The ATPase in this latter mutant appeared to be converted to a form which is resistant to the inhibitor N,N′-dicyclohexylcarbodiimide.

Original languageEnglish
Pages (from-to)217-222
Number of pages6
JournalBiochimica et Biophysica Acta - Bioenergetics
Issue number2
StatePublished - 17 Nov 1972


FundersFunder number
European Molecular Biology Organization


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