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A model for the structure of fumarate reductase in the cytoplasmic membrane of escherichia coli

✍ Scribed by Joel H. Weiner; Bernard D. Lemire; Robert W. Jones; Wayne F. Anderson; Douglas G. Scraba

Publisher
John Wiley and Sons
Year
1984
Tongue
English
Weight
707 KB
Volume
24
Category
Article
ISSN
0730-2312

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✦ Synopsis

By a recombinant DNA approach we have prepared Escherichia coli cytoplasmic membranes that are highly enriched in the terminal electron transfer enzyme fumarate reductase. This enzyme is composed of four nonidentical subunits in equal molar ratio. A 69,000-dalton covalent flavin-containing subunit and a 27,000-dalton nonheme iron-containing subunit make up a membrane extrinsic catalytic domain. Two very hydrophobic subunits of 15,000 and 13,000 daltons make up the hydrophobic membrane anchor domain. Electron microscopy of negatively stained membranes shows a characteristic knob-and-stalk-type structure composed of the catalytic domain. The anchor polypeptides have been analyzed for hydrophobic segments and alpha-helical content and a model for their organization within the lipid bilayer is presented. The results reviewed in this paper suggest a model for the fumarate reductase complex in the cytoplasmic membrane.

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