Gene fusions with β-lactamase show that subunit I of the cytochrome bd quinol oxidase from E. coli has nine transmembrane helices with the O 2 reactive site near the periplasmic surface

Jie Zhang, Blanca Barquera, Robert B. Gennis

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

The cytochrome bd quinol oxidase is a component of the respiratory chain of many prokaryotes. The enzyme contains two subunits, CydA and CydB, which were initially predicted based on the sequence of the Escherichia coli oxidase to have seven and eight transmembrane spans, respectively. More recently, the topological model of CydA was revised to predict nine transmembrane helices, based on additional sequence information from other organisms. In the current work, the topology of the E. coli oxidase was experimentally examined using β-lactamase gene fusions. The results confirm the revised topology, which places the oxygen reactive site near the periplasmic surface.

Original languageEnglish (US)
Pages (from-to)58-62
Number of pages5
JournalFEBS Letters
Volume561
Issue number1-3
DOIs
StatePublished - Mar 12 2004
Externally publishedYes

Fingerprint

Gene Fusion
Escherichia coli
Catalytic Domain
Oxidoreductases
Fusion reactions
Genes
Topology
Cytochromes
Electron Transport
Oxygen
Enzymes
cytochrome bd terminal oxidase complex, E coli
duroquinol oxidase

Keywords

  • β-Lactamase
  • Cytochrome bd
  • Gene fusion
  • Membrane protein
  • Oxidase
  • Topology

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

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abstract = "The cytochrome bd quinol oxidase is a component of the respiratory chain of many prokaryotes. The enzyme contains two subunits, CydA and CydB, which were initially predicted based on the sequence of the Escherichia coli oxidase to have seven and eight transmembrane spans, respectively. More recently, the topological model of CydA was revised to predict nine transmembrane helices, based on additional sequence information from other organisms. In the current work, the topology of the E. coli oxidase was experimentally examined using β-lactamase gene fusions. The results confirm the revised topology, which places the oxygen reactive site near the periplasmic surface.",
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AU - Zhang, Jie

AU - Barquera, Blanca

AU - Gennis, Robert B.

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N2 - The cytochrome bd quinol oxidase is a component of the respiratory chain of many prokaryotes. The enzyme contains two subunits, CydA and CydB, which were initially predicted based on the sequence of the Escherichia coli oxidase to have seven and eight transmembrane spans, respectively. More recently, the topological model of CydA was revised to predict nine transmembrane helices, based on additional sequence information from other organisms. In the current work, the topology of the E. coli oxidase was experimentally examined using β-lactamase gene fusions. The results confirm the revised topology, which places the oxygen reactive site near the periplasmic surface.

AB - The cytochrome bd quinol oxidase is a component of the respiratory chain of many prokaryotes. The enzyme contains two subunits, CydA and CydB, which were initially predicted based on the sequence of the Escherichia coli oxidase to have seven and eight transmembrane spans, respectively. More recently, the topological model of CydA was revised to predict nine transmembrane helices, based on additional sequence information from other organisms. In the current work, the topology of the E. coli oxidase was experimentally examined using β-lactamase gene fusions. The results confirm the revised topology, which places the oxygen reactive site near the periplasmic surface.

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KW - Membrane protein

KW - Oxidase

KW - Topology

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