TY  - JOUR
A1  - Reschke, Stefan
A1  - Duffus, Benjamin R.
A1  - Schrapers, Peer
A1  - Mebs, Stefan
A1  - Teutloff, Christian
A1  - Dau, Holger
A1  - Haumann, Michael
A1  - Leimkühler, Silke
T1  - Identification of YdhV as the First Molybdoenzyme Binding a Bis-Mo-MPT Cofactor in Escherichia coli
T2  - Biochemistry
N2  - The oxidoreductase YdhV in Escherichia coli has been predicted to belong to the family of molybdenum/tungsten cofactor (Moco/Wco)-containing enzymes. In this study, we characterized the YdhV protein in detail, which shares amino acid sequence homology with a tungsten-containing benzoyl-CoA reductase binding the bis-W-MPT (for metal-binding pterin) cofactor. The cofactor was identified to be of a bis-Mo-MPT type with no guanine nucleotides present, which represents a form of Moco that has not been found previously in any molybdoenzyme. Our studies showed that YdhV has a preference for bis-Mo-MPT over bis-W-MPT to be inserted into the enzyme. In-depth characterization of YdhV by X-ray absorption and electron paramagnetic resonance spectroscopies revealed that the bis-Mo-MPT cofactor in YdhV is redox active. The bis-Mo-MPT and bis-W-MPT cofactors include metal centers that bind the four sulfurs from the two dithiolene groups in addition to a cysteine and likely a sulfido ligand. The unexpected presence of a bis-Mo-MPT cofactor opens an additional route for cofactor biosynthesis in E. coli and expands the canon of the structurally highly versatile molybdenum and tungsten cofactors.
Y1  - 2019
UR  - https://publishup.uni-potsdam.de/frontdoor/index/index/docId/49692
SN  - 0006-2960
VL  - 58
IS  - 17
SP  - 2228
EP  - 2242
PB  - American Chemical Society
CY  - Washington
ER  -