A predicted structure of the cytochrome c oxidase from Burkholderia pseudomallei

Mohd Firdaus Mohd Raih, Ahmad Tarmidi Sailan, Zulkeflie Zamrod, Mohammed Noor Embi, Rahmah Mohamed

Research output: Contribution to journalArticle

Abstract

Cytochrome c oxidase, the terminal enzyme of the respiratory chains of mitochondria and aerobic bacteria, catalyzes electron transfer from cytochrome c to molecular oxygen. The enzyme belongs to the haem-copper-containing oxidases superfamily. A recombinant plasmid carrying a 2.0 kb insert from a Burkholderia pseudomallei genomic library was subjected to automated DNA sequencing utilizing a primer walking strategy. Analysis of the 2002 bp insert revealed a 1536 bp open reading frame predicted to encode a putative cytochrome c oxidase. Further analysis using sequence alignments and tertiary structure analysis tools demonstrated that the hypothetical B. pseudomallei cytochrome c oxidase is similar to cytochrome c oxidases from other organisms such as Thermus thermophilus (36% protein sequence identity), Paracoccus denitrificans and bovine heart mitochondrial, the latter two which crystal structures available. The deduced 512 residue protein sequence includes the six canonical histidine residues involved in binding the low spin heme B and the binuclear center CuB/hemeA. The predicted tertiary structure of the hypothetical protein is consistent with previous models of electron transfer for cytochrome c oxidase.

Original languageEnglish
Pages (from-to)18-25
Number of pages8
JournalElectronic Journal of Biotechnology
Volume6
Issue number1
Publication statusPublished - 15 Apr 2003

Fingerprint

Burkholderia pseudomallei
Electron Transport Complex IV
Heme
Paracoccus denitrificans
Electrons
Thermus thermophilus
Aerobic Bacteria
Genomic Library
Sequence Alignment
Enzymes
Electron Transport
Cytochromes c
Tertiary Protein Structure
DNA Sequence Analysis
Histidine
Open Reading Frames
Walking
Mitochondria
Proteins
Plasmids

Keywords

  • Burkholderia pseudomallei
  • Cytochrome c oxidase
  • Protein structure prediction
  • Sequence alignments
  • Structure-function extrapolation

ASJC Scopus subject areas

  • Biotechnology

Cite this

A predicted structure of the cytochrome c oxidase from Burkholderia pseudomallei. / Mohd Raih, Mohd Firdaus; Sailan, Ahmad Tarmidi; Zamrod, Zulkeflie; Embi, Mohammed Noor; Mohamed, Rahmah.

In: Electronic Journal of Biotechnology, Vol. 6, No. 1, 15.04.2003, p. 18-25.

Research output: Contribution to journalArticle

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AB - Cytochrome c oxidase, the terminal enzyme of the respiratory chains of mitochondria and aerobic bacteria, catalyzes electron transfer from cytochrome c to molecular oxygen. The enzyme belongs to the haem-copper-containing oxidases superfamily. A recombinant plasmid carrying a 2.0 kb insert from a Burkholderia pseudomallei genomic library was subjected to automated DNA sequencing utilizing a primer walking strategy. Analysis of the 2002 bp insert revealed a 1536 bp open reading frame predicted to encode a putative cytochrome c oxidase. Further analysis using sequence alignments and tertiary structure analysis tools demonstrated that the hypothetical B. pseudomallei cytochrome c oxidase is similar to cytochrome c oxidases from other organisms such as Thermus thermophilus (36% protein sequence identity), Paracoccus denitrificans and bovine heart mitochondrial, the latter two which crystal structures available. The deduced 512 residue protein sequence includes the six canonical histidine residues involved in binding the low spin heme B and the binuclear center CuB/hemeA. The predicted tertiary structure of the hypothetical protein is consistent with previous models of electron transfer for cytochrome c oxidase.

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