Abstract
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. Structured summary of protein interactions cydA physically interacts with cydB by affinity technology (View interaction) cydA physically interacts with cydB by molecular sieving (View interaction) cydB, cydA and cydX physically interact by molecular sieving (View interaction) cydB, cydA, and cydX physically interacts by affinity technology (1, 2)
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1537-1541 |
| Number of pages | 5 |
| Journal | FEBS Letters |
| Volume | 588 |
| Issue number | 9 |
| DOIs | |
| State | Published - May 2 2014 |
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Keywords
- CydAB
- CydX
- Escherichia coli
- UV/vis difference spectroscopy
- Ubiquinol cytochrome bd oxidase
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
Cite this
Subunit CydX of Escherichia coli cytochrome bd ubiquinol oxidase is essential for assembly and stability of the di-heme active site. / Hoeser, Jo; Hong, Sangjin; Gehmann, Gerfried; Gennis, Robert B.; Friedrich, Thorsten.
In: FEBS Letters, Vol. 588, No. 9, 02.05.2014, p. 1537-1541.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Subunit CydX of Escherichia coli cytochrome bd ubiquinol oxidase is essential for assembly and stability of the di-heme active site
AU - Hoeser, Jo
AU - Hong, Sangjin
AU - Gehmann, Gerfried
AU - Gennis, Robert B.
AU - Friedrich, Thorsten
PY - 2014/5/2
Y1 - 2014/5/2
N2 - 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. Structured summary of protein interactions cydA physically interacts with cydB by affinity technology (View interaction) cydA physically interacts with cydB by molecular sieving (View interaction) cydB, cydA and cydX physically interact by molecular sieving (View interaction) cydB, cydA, and cydX physically interacts by affinity technology (1, 2)
AB - 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. Structured summary of protein interactions cydA physically interacts with cydB by affinity technology (View interaction) cydA physically interacts with cydB by molecular sieving (View interaction) cydB, cydA and cydX physically interact by molecular sieving (View interaction) cydB, cydA, and cydX physically interacts by affinity technology (1, 2)
KW - CydAB
KW - CydX
KW - Escherichia coli
KW - UV/vis difference spectroscopy
KW - Ubiquinol cytochrome bd oxidase
UR - http://www.scopus.com/inward/record.url?scp=84899643926&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84899643926&partnerID=8YFLogxK
U2 - 10.1016/j.febslet.2014.03.036
DO - 10.1016/j.febslet.2014.03.036
M3 - Article
C2 - 24681096
AN - SCOPUS:84899643926
VL - 588
SP - 1537
EP - 1541
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 9
ER -