Molecular Genetic and Protein Chemical Characterization of the Cytochrome ba3 from Thermus thermophilus HB8 (∗)

Thermus thermophilus HB8 cells grown under reduced dioxygen tensions contain a substantially increased amount of heme A, much of which appears to be due to the presence of the terminal oxidase, cytochrome ba3. We describe a purification procedure for this enzyme that yields ∼100 mg of pure protein f...

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Veröffentlicht in:	The Journal of biological chemistry 1995-09, Vol.270 (35), p.20345-20358
Hauptverfasser:	Keightley, J. Andrew, Zimmermann, Barbara H., Mather, Michael W., Springer, Penelope, Pastuszyn, Andrzej, Lawrence, David M., Fee, James A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Base Sequence Binding Sites Chromatography, High Pressure Liquid Cloning, Molecular Codon Copper - metabolism Cytochrome b Group - biosynthesis Cytochrome b Group - chemistry Cytochrome b Group - genetics DNA, Bacterial - chemistry DNA, Bacterial - metabolism Electron Transport Complex IV - biosynthesis Electron Transport Complex IV - chemistry Electron Transport Complex IV - genetics Genes, Bacterial Humans Hydrogen Bonding Macromolecular Substances Molecular Sequence Data Molecular Weight Oligonucleotide Probes Protein Structure, Secondary Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Restriction Mapping Sequence Homology, Amino Acid Thermus thermophilus - genetics Thermus thermophilus - growth & development Thermus thermophilus - metabolism
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