Meny

Javascript is not activated in your browser. This website needs javascript activated to work properly.
Du är här

Bacillus subtilis ResA is a thiol-disulfide oxidoreductase involved in cytochrome c synthesis

Författare:
Publiceringsår: 2003
Språk: Engelska
Sidor: 17852-17858
Publikation/Tidskrift/Serie: Journal of Biological Chemistry
Volym: 278
Nummer: 20
Dokumenttyp: Artikel
Förlag: American Society for Biochemistry and Molecular Biology, Inc.

Sammanfattning

Covalent attachment of heme to apocytochromes c in bacteria occurs on the outside of the cytoplasmic membrane and requires two reduced cysteinyls at the heme binding site. A constructed ResA-deficient Bacillus subtilis strain was found to lack c-type cytochromes. Cytochrome c synthesis was restored in the mutant by: (i) in trans expression of resA; (ii) deficiency in BdbD, a thioldisulfide oxidoreductase that catalyzes formation of an intramolecular disulfide bond in apocytochrome c after transfer of the polypeptide across the cytoplasmic membrane; or (iii) by addition of the reductant dithiothreitol to the growth medium. In vivo studies of ResA showed that it is membrane-associated with its thioredoxin-like domain on the outside of the cytoplasmic membrane. Analysis of a soluble form of the protein revealed two redox reactive cysteine residues with a midpoint potential of about -340 mV at pH 7. We conclude that ResA, probably together with another thiol-disulfide oxidoreductase, CcdA, is required for the reduction of the cysteinyls in the heme binding site of apocytochrome c.

Disputation

Nyckelord

  • Biology and Life Sciences

Övriga

Published
Yes
  • ISSN: 0021-9258

Box 117, 221 00 LUND
Telefon 046-222 00 00 (växel)
Telefax 046-222 47 20
lu [at] lu [dot] se

Fakturaadress: Box 188, 221 00 LUND
Organisationsnummer: 202100-3211
Om webbplatsen