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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)

Abstract

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
OAI identifier: oai:figshare.com:article/8006480
Provided by: FigShare
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