- Subunit CydX of Escherichia coli cytochrome bd ubiquinol oxidase is essential for assembly and stability of the di-heme active site.
Subunit CydX of Escherichia coli cytochrome bd ubiquinol oxidase is essential for assembly and stability of the di-heme active site.
FEBS letters (2014-04-01)
Jo Hoeser, Sangjin Hong, Gerfried Gehmann, Robert B Gennis, Thorsten Friedrich
PMID24681096
RESUMEN
Cytochrome bd ubiquinol oxidase uses the electron transport from ubiquinol to oxygen to establish a proton gradient across the membrane. The enzyme complex consists of subunits CydA and B and contains two b- and one d-type hemes as cofactors. Recently, it was proposed that a third subunit named CydX is essential for the function of the complex. Here, we show that CydX is indeed a subunit of purified Escherichia coli cytochrome bd oxidase and that the small protein is needed either for the assembly or the stability of the active site di-heme center and, thus, is essential for oxidase activity.
MATERIALES
Referencia del producto
Marca
Descripción del producto
Sigma-Aldrich
(Hydroxypropyl)methyl cellulose, viscosity 2,600-5,600 cP, 2 % in H2O(20 °C)(lit.)