A predicted structure of the cytochrome c oxidase from Burkholderia pseudomallei

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 Bu...

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Autores principales: Mohd. Raih,Mohd. Firdaus, Sailan,Ahmad Tarmidi, Zamrod,Zulkeflie, Embi,Mohd. Noor, Mohamed,Rahmah
Lenguaje:English
Publicado: Pontificia Universidad Católica de Valparaíso 2003
Acceso en línea:http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582003000100005
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spelling oai:scielo:S0717-345820030001000052003-08-18A predicted structure of the cytochrome c oxidase from Burkholderia pseudomalleiMohd. Raih,Mohd. FirdausSailan,Ahmad TarmidiZamrod,ZulkeflieEmbi,Mohd. NoorMohamed,Rahmah 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.info:eu-repo/semantics/openAccessPontificia Universidad Católica de ValparaísoElectronic Journal of Biotechnology v.6 n.1 20032003-04-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582003000100005en
institution Scielo Chile
collection Scielo Chile
language English
description 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.
author Mohd. Raih,Mohd. Firdaus
Sailan,Ahmad Tarmidi
Zamrod,Zulkeflie
Embi,Mohd. Noor
Mohamed,Rahmah
spellingShingle Mohd. Raih,Mohd. Firdaus
Sailan,Ahmad Tarmidi
Zamrod,Zulkeflie
Embi,Mohd. Noor
Mohamed,Rahmah
A predicted structure of the cytochrome c oxidase from Burkholderia pseudomallei
author_facet Mohd. Raih,Mohd. Firdaus
Sailan,Ahmad Tarmidi
Zamrod,Zulkeflie
Embi,Mohd. Noor
Mohamed,Rahmah
author_sort Mohd. Raih,Mohd. Firdaus
title A predicted structure of the cytochrome c oxidase from Burkholderia pseudomallei
title_short A predicted structure of the cytochrome c oxidase from Burkholderia pseudomallei
title_full A predicted structure of the cytochrome c oxidase from Burkholderia pseudomallei
title_fullStr A predicted structure of the cytochrome c oxidase from Burkholderia pseudomallei
title_full_unstemmed A predicted structure of the cytochrome c oxidase from Burkholderia pseudomallei
title_sort predicted structure of the cytochrome c oxidase from burkholderia pseudomallei
publisher Pontificia Universidad Católica de Valparaíso
publishDate 2003
url http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582003000100005
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