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The chaperone FdsC for Rhodobacter capsulatus formate dehydrogenase binds the bis-molybdopterin guanine dinucleotide cofactor

  • Molybdoenzymes are complex enzymes in which the molybdenum cofactor (Moco) is deeply buried in the enzyme. Most molybdoenzymes contain a specific chaperone for the insertion of Moco. For the formate dehydrogenase FdsGBA from Rhodobacter capsulatus the two chaperones FdsC and FdsD were identified to be essential for enzyme activity, but are not a subunit of the mature enzyme. Here, we purified and characterized the FdsC protein after heterologous expression in Escherichia coli. We were able to copurify FdsC with the bound Moco derivate bis-molybdopterin guanine dinucleotide. This cofactor successfully was used as a source to reconstitute the activity of molybdoenzymes. Structured summary of protein interactions: FdsC and FdsC bind by molecular sieving (View interaction) FdsD binds to RcMobA by surface plasmon resonance (View interaction) FdsC binds to RcMobA by surface plasmon resonance (View interaction) FdsC binds to FdsA by surface plasmon resonance (View interaction)

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Author:Nadine Boehmer, Tobias Hartmann, Silke Leimkuehler
ISSN:0014-5793 (print)
ISSN:1873-3468 (online)
Pubmed Id:http://www.ncbi.nlm.nih.gov/pubmed?term=24444607
Parent Title (English):FEBS letters : the journal for rapid publication of short reports in molecular biosciences
Place of publication:Amsterdam
Document Type:Article
Year of first Publication:2014
Year of Completion:2014
Release Date:2017/03/27
Tag:Chaperone; Formate dehydrogenase; L-cysteine desulfurase; Molybdenum cofactor; bis-MGD
First Page:531
Last Page:537
Funder:DFG [LE1171/6-1]; DFG cluster of excellence [EXC314]
Organizational units:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie
Peer Review:Referiert