title: Exploiting the versatility and selectivity of Mo enzymes with electrochemistry.
abstract: This article covers recent advances in the electrochemical study of the mononuclear molybdenum enzymes. Virtually all of these enzymes catalyse a coupled 2-electron, O-atom transfer reaction on a substrate of either organic or inorganic origin. There is a remarkable commonality in structure, function and mechanism of the mononuclear Mo enzymes despite the diversity of their substrates; many that are important to environmental monitoring, food quality control and biomedical science. Mo enzymes routinely oxidise or reduce otherwise inert substrates for which there exist no rapid, simple and reliable analytical methods for their determination and as such represent a potentially rich source of proteins that may be applied in electrochemical biosensors.
authors.affiliation: Centre for Metals in Biology, School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane 4072, Australia. p.bernhardt@uq.edu.au
authors.forename: Paul V
authors.initials: PV
authors.lastname: Bernhardt
mesh_terms: D055162:Biocatalysis; D015374:Biosensing Techniques / Q000379:methods*; D020134:Catalytic Domain; D004563:Electrochemistry; D004579:Electron Transport; D004583:Electrons; D004798:Enzymes / Q000737:chemistry* / Q000145:classification / Q000378:metabolism; D008956:Models, Chemical; D008982:Molybdenum / Q000737:chemistry* / Q000378:metabolism; D009942:Organometallic Compounds / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism; D010088:Oxidoreductases / Q000737:chemistry / Q000378:metabolism; D010105:Oxygenases / Q000737:chemistry / Q000378:metabolism
chemical_list: D004798:Enzymes; D009942:Organometallic Compounds; D008982:Molybdenum; D010088:Oxidoreductases; D010105:Oxygenases