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. 1983 Oct;156(1):115–121. doi: 10.1128/jb.156.1.115-121.1983

Immunological characterization of an Escherichia coli strain which is lacking cytochrome d.

R G Kranz, C A Barassi, M J Miller, G N Green, R B Gennis
PMCID: PMC215058  PMID: 6311794

Abstract

The isolated membranes from an Escherichia coli mutant strain which lacks spectroscopically detectable levels of cytochromes d, a1, and b558 also have abnormally low levels of N,N,N',N'-tetramethyl-p-phenylenediamine oxidase activity. In this paper, it is shown that the material previously identified as the N,N,N',N'-tetramethyl-p-phenylenediamine oxidase is, in fact, the two-subunit cytochrome d complex. Antisera directed against the native cytochrome d complex as well as against each of two subunits apparent on sodium dodecyl sulfate-polyacrylamide gels were used to show that the mutant strain lacks both subunits of the cytochrome d complex. Introduction of F-prime F152 into the mutant strain restored the two subunits along with the spectroscopic and enzymatic activity associated with the cytochrome d complex.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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