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Respiratory proteins from the extremely thermophilic aerobic bacterium, thermus-thermophilus - purification procedures for cytochrome-c552, cytochrome-c555,549, and cytochrome-c1aa3 and chemical evidence for a single subunit cytochrome-aa3

Academic Article
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Overview

authors

  • Yoshida, T.
  • Lorence, R. M.
  • Choc, M. G.
  • Tarr, G. E.
  • Findling, K. L.
  • Fee, James

publication date

  • 1984

journal

  • Journal of Biological Chemistry  Journal

abstract

  • We have developed a chemically defined, minimal growth medium for Thermus thermophilus which is suitable for nutritional studies, isotopic enrichment, and genetic manipulation of the organism. Reliable procedures are described for the large scale purification of cytochrome c552 from the periplasm and for cytochrome c555,549 and cytochrome c1 aa3 from the plasma membrane. In contrast to a previous report (Fee, J. A., Choc, M. G., Findling, K. L., Lorence, R., and Yoshida, T. (1980) Proc. Natl. Acad. Sci. U. S. A. 77, 147-151) which suggested a molecular weight near 200,000, the cytochrome c1aa3 complex was shown by protein and amino acid analyses to have Mr approximately 93,000. Sodium dodecyl sulfate-urea-polyacrylamide gel electrophoresis and reversed phase high performance liquid chromatography, combined with amino acid analyses, revealed the presence of only two proteins in a 1:1 ratio: C-protein has Mr approximately 33,000, binds heme C, and is thought to correspond to cytochrome c1. A-protein has Mr approximately 55,000 and is thought to bind the four redox components (2 heme A and 2 Cu) of cytochrome aa3.

subject areas

  • Amino Acids
  • Animals
  • Cattle
  • Cytochrome c Group
  • Electron Transport Complex IV
  • Horses
  • Macromolecular Substances
  • Molecular Weight
  • Oxygen Consumption
  • Thermus
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

PubMed ID

  • 6323398
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Additional Document Info

start page

  • 112

end page

  • 123

volume

  • 259

issue

  • 1

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