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  Presence and role of a second disulphide bond in recombinant lupanine hydroxylase using site-directed mutagenesis with (143)Cys -> Ser and (124,143)Cys -> Ser mutations in Escherichia coli

Stampolidis, P., Kaderbhai, N. N., & Kaderbhai, M. A. (2012). Presence and role of a second disulphide bond in recombinant lupanine hydroxylase using site-directed mutagenesis with (143)Cys -> Ser and (124,143)Cys -> Ser mutations in Escherichia coli. FEMS Microbiology Letters, 334(1), 35-43.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0010-5174-7 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0010-5175-5
Genre: Journal Article
Alternative Title : FEMS Microbiol. Lett.

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 Creators:
Stampolidis, P.1, Author           
Kaderbhai, N. N., Author
Kaderbhai, M. A., Author
Affiliations:
1Ullrich, Axel / Molecular Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565172              

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Free keywords: protein export; periplasmic space; disulphide bond formation; quinocytochrome c; pyrroloquinoline quinone; quinohaemoprotein
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Language(s): eng - English
 Dates: 2012-09
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 619190
ISI: 000307007200005
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Title: FEMS Microbiology Letters
  Alternative Title : FEMS Microbiol. Lett.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: HOBOKEN : WILEY-BLACKWELL
Pages: - Volume / Issue: 334 (1) Sequence Number: - Start / End Page: 35 - 43 Identifier: ISSN: 0378-1097