TY  - JOUR
A1  - Badalyan, Artavazd
A1  - Neumann-Schaal, Meina
A1  - Leimkühler, Silke
A1  - Wollenberger, Ursula
T1  - A Biosensor for aromatic aldehydes comprising the mediator dependent PaoABC-Aldehyde oxidoreductase
JF  - Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis
N2  - A novel aldehyde oxidoreductase (PaoABC) from Escherichia coli was utilized for the development of an oxygen insensitive biosensor for benzaldehyde. The enzyme was immobilized in polyvinyl alcohol and currents were measured for aldehyde oxidation with different one and two electron mediators with the highest sensitivity for benzaldehyde in the presence of hexacyanoferrate(III). The benzaldehyde biosensor was optimized with respect to mediator concentration, enzyme loading and pH using potassium hexacyanoferrate(III). The linear measuring range is between 0.5200 mu M benzaldehyde. In correspondence with the substrate selectivity of the enzyme in solution the biosensor revealed a preference for aromatic aldehydes and less effective conversion of aliphatic aldehydes. The biosensor is oxygen independent, which is a particularly attractive feature for application. The biosensor can be applied to detect contaminations with benzaldehyde in solvents such as benzyl alcohol, where traces of benzaldehyde in benzyl alcohol down to 0.0042?% can be detected.
KW  - Aldehyde oxidoreductase
KW  - Benzaldehyde
KW  - Biosensor
KW  - Aromatic aldehydes
KW  - Molybdenum cofactor
Y1  - 2013
U6  - https://doi.org/10.1002/elan.201200362
SN  - 1040-0397
VL  - 25
IS  - 1
SP  - 101
EP  - 108
PB  - Wiley-VCH
CY  - Weinheim
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  -