Subunit CydX of Escherichia coli cytochrome bd ubiquinol oxidase is essential for assembly and stability of the di-heme active site

Jo Hoeser, Sangjin Hong, Gerfried Gehmann, Robert B. Gennis, Thorsten Friedrich

Research output: Contribution to journalArticle

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 languageEnglish (US)
Pages (from-to)1537-1541
Number of pages5
JournalFEBS Letters
Volume588
Issue number9
DOIs
StatePublished - May 2 2014

Fingerprint

Cytochromes
Heme
Escherichia coli
Catalytic Domain
Technology
Electron Transport Complex IV
Electron Transport
Protons
Oxidoreductases
Proteins
Oxygen
Membranes
Enzymes
ubiquinol oxidase
heme d
ubiquinol

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 journalArticle

Hoeser, Jo ; Hong, Sangjin ; Gehmann, Gerfried ; Gennis, Robert B. ; Friedrich, Thorsten. / Subunit CydX of Escherichia coli cytochrome bd ubiquinol oxidase is essential for assembly and stability of the di-heme active site. In: FEBS Letters. 2014 ; Vol. 588, No. 9. pp. 1537-1541.
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AU - Hong, Sangjin

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AU - Gennis, Robert B.

AU - Friedrich, Thorsten

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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)

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