Article
Two hydrophobic subunits are essential for the heme b ligation and functional assembly of complex II (succinate-ubiquinone oxidoreductase) from Escherichia coli.
The Journal of biological chemistry - 5 Jan 1996
Nakamura K, Yamaki M, Sarada M, Nakayama S, Vibat C R, Gennis R B, Nakayashiki T, Inokuchi H, Kojima S, Kita K
Abstract excerpt
Complex II (succinate-ubiquinone oxidoreductase) from Escherichia coli is composed of four nonidentical subunits encoded by the sdhCDAB operon. Gene products of sdhC and sdhD are small hydrophobic subunits that anchor the hydrophilic catalytic subunits (flavoprotein and iron-sulfur protein) to the cytoplasmic membrane and are believed to be the components of cytochrome b556 in E. coli complex II. In the present...
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