Mutants of Escherichia coli lacking disulphide oxidoreductases DsbA and DsbB cannot synthesise an exogenous monohaem c-type cytochrome except in the presence of disulphide compounds.

doi:10.1016/s0014-5793(96)01256-2

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Article

Mutants of Escherichia coli lacking disulphide oxidoreductases DsbA and DsbB cannot synthesise an exogenous monohaem c-type cytochrome except in the presence of disulphide compounds.

FEBS letters - 2 Dec 1996

Sambongi Y, Ferguson S J

Abstract excerpt

Absence through mutation of two proteins involved in periplasmic disulphide bond formation, DsbA and DsbB, results in failure of anaerobically grown Escherichia coli to synthesise the holo forms of either its endogenous c-type cytochrome nitrite reductase or exogenous cytochrome c550 from Paracoc...

Topics

Alkaline Phosphatase
Bacterial Proteins
Culture Media
Cytochrome c Group
Escherichia coli
Glutathione
Isomerases
Membrane Proteins
Mutation
Oxidation-Reduction
Protein Disulfide-Isomerases

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