TY  - JOUR
A1  - Tiedemann, Kim
A1  - Iobbi-Nivol, Chantal
A1  - Leimkühler, Silke
T1  - The Role of the Nucleotides in the Insertion of the bis-Molybdopterin Guanine Dinucleotide Cofactor into apo-Molybdoenzymes
JF  - Molecules
N2  - The role of the GMP nucleotides of the bis-molybdopterin guanine dinucleotide (bis-MGD) cofactor of the DMSO reductase family has long been a subject of discussion. The recent characterization of the bis-molybdopterin (bis-Mo-MPT) cofactor present in the E. coli YdhV protein, which differs from bis-MGD solely by the absence of the nucleotides, now enables studying the role of the nucleotides of bis-MGD and bis-MPT cofactors in Moco insertion and the activity of molybdoenzymes in direct comparison. Using the well-known E. coli TMAO reductase TorA as a model enzyme for cofactor insertion, we were able to show that the GMP nucleotides of bis-MGD are crucial for the insertion of the bis-MGD cofactor into apo-TorA.
KW  - bis-MGD
KW  - chaperone
KW  - molybdenum cofactor
KW  - TMAO reductase
Y1  - 2022
U6  - https://doi.org/10.3390/molecules27092993
SN  - 1420-3049
VL  - 27
SP  - 1
EP  - 15
PB  - MDPI
CY  - Basel, Schweiz
ET  - 9
ER  - 
TY  - JOUR
A1  - Boehmer, Nadine
A1  - Hartmann, Tobias
A1  - Leimkühler, Silke
T1  - The chaperone FdsC for Rhodobacter capsulatus formate dehydrogenase binds the bis-molybdopterin guanine dinucleotide cofactor
JF  - FEBS letters : the journal for rapid publication of short reports in molecular biosciences
N2  - 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)
KW  - Molybdenum cofactor
KW  - L-cysteine desulfurase
KW  - Formate dehydrogenase
KW  - Chaperone
KW  - bis-MGD
Y1  - 2014
U6  - https://doi.org/10.1016/j.febslet.2013.12.033
SN  - 0014-5793
SN  - 1873-3468
VL  - 588
IS  - 4
SP  - 531
EP  - 537
PB  - Elsevier
CY  - Amsterdam
ER  -