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Identification of YdhV as the First Molybdoenzyme Binding a Bis-Mo-MPT Cofactor in <i>Escherichia coli</i>

By Stefan Reschke (1625572), Benjamin R. Duffus (1876399), Peer Schrapers (1625575), Stefan Mebs (1455724), Christian Teutloff (498027), Holger Dau (1625578), Michael Haumann (1455718) and Silke Leimkühler (1327842)


The oxidoreductase YdhV in <i>Escherichia coli</i> 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 <i>E. coli</i> and expands the canon of the structurally highly versatile molybdenum and tungsten cofactors

Topics: Biophysics, Biochemistry, Medicine, Microbiology, Cell Biology, Molecular Biology, Biotechnology, Evolutionary Biology, Sociology, Immunology, Infectious Diseases, Plant Biology, Computational Biology, Biological Sciences not elsewhere classified, Chemical Sciences not elsewhere classified, First Molybdoenzyme Binding, bis-Mo-MPT cofactor, tungsten-containing benzoyl-CoA reductase binding, acid sequence homology, Escherichia coli, bis-W-MPT, YdhV
Year: 2019
DOI identifier: 10.1021/acs.biochem.9b00078.s001
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Provided by: FigShare
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