6-S-Cysteinylation of bi-covalently attached FAD in berberine bridge enzyme tunes the redox potential for optimal activity

Research output: Contribution to journalArticleResearchpeer-review

Original languageEnglish
Pages (from-to)24437-24443
JournalThe Journal of Biological Chemistry
Volume282
Issue number33
Publication statusPublished - 2007

Treatment code (Nähere Zuordnung)

  • Basic - Fundamental (Grundlagenforschung)

Cite this

6-S-Cysteinylation of bi-covalently attached FAD in berberine bridge enzyme tunes the redox potential for optimal activity. / Winkler, Andreas; Kutchan, Toni M.; Macheroux, Peter.

In: The Journal of Biological Chemistry, Vol. 282, No. 33, 2007, p. 24437-24443.

Research output: Contribution to journalArticleResearchpeer-review

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title = "6-S-Cysteinylation of bi-covalently attached FAD in berberine bridge enzyme tunes the redox potential for optimal activity",
author = "Andreas Winkler and Kutchan, {Toni M.} and Peter Macheroux",
year = "2007",
language = "English",
volume = "282",
pages = "24437--24443",
journal = "The Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "33",

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T1 - 6-S-Cysteinylation of bi-covalently attached FAD in berberine bridge enzyme tunes the redox potential for optimal activity

AU - Winkler, Andreas

AU - Kutchan, Toni M.

AU - Macheroux, Peter

PY - 2007

Y1 - 2007

M3 - Article

VL - 282

SP - 24437

EP - 24443

JO - The Journal of Biological Chemistry

JF - The Journal of Biological Chemistry

SN - 0021-9258

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