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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
2001-1-9
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pubmed:databankReference |
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pubmed:abstractText |
The bax-type cytochrome c oxidase from Thermus thermophilus is known as a two subunit enzyme. Deduced from the crystal structure of this enzyme, we discovered the presence of an additional transmembrane helix "subunit IIa" spanning the membrane. The hydrophobic N-terminally blocked protein was isolated in high yield using high-performance liquid chromatography. Its complete amino acid sequence was determined by a combination of automated Edman degradation of both the deformylated and the cyanogen bromide cleaved protein and automated C-terminal sequencing of the native protein. The molecular mass of 3,794 Da as determined by MALDI-MS and by ESI requires the N-terminal methionine to be formylated and is in good agreement with the value calculated from the formylmethionine containing sequence (3,766.5 Da + 28 Da = 3,794.5 Da). This subunit consits of 34 residues forming one helix across the membrane (Lys5-Ala34), which corresponds in space to the first transmembrane helix of subunit II of the cytochrome c oxidases from Paracoccus denitrificans and bovine heart, however, with opposite polarity. It is 35% identical to subunit IV of the ba3-cytochrome oxidase from Natronobacterium pharaonis. The open reading frame encoding this new subunit IIa (cbaD) is located upstream of cbaB in the same operon as the genes for subunit I (cbaA) and subunit II (cbaB).
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11152118-10338009,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11152118-10775261,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11152118-1372250,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11152118-2199797,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11152118-2842747,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11152118-4472379,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11152118-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11152118-6059350,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11152118-6244539,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11152118-7615066,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11152118-7651515,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11152118-7652554,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11152118-7657607,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11152118-7984110,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11152118-8063781,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11152118-8083153,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11152118-8578586,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11152118-8638158,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11152118-9281430,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11152118-9299406,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11152118-9380672,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11152118-9428682,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11152118-9582433,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11152118-9624044,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11152118-9894002
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0961-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2068-73
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:11152118-Amino Acid Sequence,
pubmed-meshheading:11152118-Animals,
pubmed-meshheading:11152118-Cattle,
pubmed-meshheading:11152118-Chromatography, High Pressure Liquid,
pubmed-meshheading:11152118-Cyanogen Bromide,
pubmed-meshheading:11152118-Cytochrome b Group,
pubmed-meshheading:11152118-Electron Transport Complex IV,
pubmed-meshheading:11152118-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:11152118-Methionine,
pubmed-meshheading:11152118-Models, Genetic,
pubmed-meshheading:11152118-Models, Molecular,
pubmed-meshheading:11152118-Molecular Sequence Data,
pubmed-meshheading:11152118-Myocardium,
pubmed-meshheading:11152118-Open Reading Frames,
pubmed-meshheading:11152118-Protein Structure, Tertiary,
pubmed-meshheading:11152118-Sequence Homology, Amino Acid,
pubmed-meshheading:11152118-Spectrometry, Mass, Electrospray Ionization,
pubmed-meshheading:11152118-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:11152118-Thermus thermophilus
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pubmed:year |
2000
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pubmed:articleTitle |
Primary structure of a novel subunit in ba3-cytochrome oxidase from Thermus thermophilus.
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pubmed:affiliation |
Rheinisch-Westfälische Technische Hochschule Aachen, Institut für Biochemie, Germany. tsoulimane@post.klinikum.rwth-aachen.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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