Oxidative phosphorylation in mutants of Escherichia coli defective in energy transduction

D. L. Gutnick; B. I. Kanner; P. W. Postma

doi:10.1016/0005-2728(72)90237-X

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

Biotechnology

Research output: Contribution to journal › Article › peer-review

32 Scopus citations

Abstract

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 language	English
Pages (from-to)	217-222
Number of pages	6
Journal	Biochimica et Biophysica Acta - Bioenergetics
Volume	283
Issue number	2
DOIs	https://doi.org/10.1016/0005-2728(72)90237-X
State	Published - 17 Nov 1972

Funding

Funders	Funder number
European Molecular Biology Organization

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10.1016/0005-2728(72)90237-X

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title = "Oxidative phosphorylation in mutants of Escherichia coli defective in energy transduction",

abstract = "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.",

author = "Gutnick, {D. L.} and Kanner, {B. I.} and Postma, {P. W.}",

note = "Funding Information: We wish to thank Mrs Vanda Froidis and Mrs Digna voor in't Holt for expert technical assistance and Dr Karel van Dam for his critical reading of the manuscript. One of us (D.L.G.) was supported by a grant from the European Molecular Biology Organization.",

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PY - 1972/11/17

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N2 - 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.

AB - 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.

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Oxidative phosphorylation in mutants of Escherichia coli defective in energy transduction

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