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Mutants of Escherichia coli K12 Defective in Oxidative Phosphorylation

Hans Ulrich Schairer, Dorothee Gruber

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Abstract

A mutant of Escherichia coli K12 has been isolated with a defect in oxidative phosphorylation. Though the mutation does not affect the activity of the Mg2+, Ca2+ ‐activated ATPase the mutant strain does not show ATP‐dependent transhydrogenase activity. Also, in contrast to the wild‐type strain, active β‐galactoside transport is abolished after inhibition of respiration by cyanide. Mapping of the mutation locus shows that it lies between asn and ilv on the E. coli chromosome.

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What this paper is about

A mutant of Escherichia coli K12 has been isolated with a defect in oxidative phosphorylation. Though the mutation does not affect the activity of the Mg2+, Ca2+ ‐activated ATPase the mutant strain does not show ATP‐dependent transhydrogenase activity. Also, in contrast to the wild‐type strain, active β‐galactoside transport is abolished after inhibition of respiration by cyanide. Mapping of the mutation locus shows that it lies between asn and ilv on the E. coli chromosome.

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Available abstract

A mutant of Escherichia coli K12 has been isolated with a defect in oxidative phosphorylation. Though the mutation does not affect the activity of the Mg2+, Ca2+ ‐activated ATPase the mutant strain does not show ATP‐dependent transhydrogenase activity. Also, in contrast to the wild‐type strain, active β‐galactoside transport is abolished after inhibition of respiration by cyanide. Mapping of the mutation locus shows that it lies between asn and ilv on the E. coli chromosome.

Key concepts: Escherichia coli, Oxidative phosphorylation, Mutant, Phosphorylation, Biochemistry, Mutation, Uncoupling Agents, Strain (injury)

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