Year: 1983
Type: article
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.
Source: Journal of Bacteriology
Authors: R G Kranz, C A Barassi, M J Miller, G N Green, R B Gennis
Institution: University of Illinois Urbana-Champaign
Language: English
Subfield: Genetics
Domain: Life Sciences
Open Access status: bronze
OpenAlex ID: W1854690049