Abstract

Molybdenum (Mo) is an essential micronutrient for the majority of organisms ranging from bacteria to animals. To fulfil its biological role, it is incorporated into a pterin-based Mo-cofactor (Moco) and can be found in the active centre of more than 50 enzymes that are involved in key reactions of carbon, nitrogen and sulfur metabolism. Five of the Mo-enzymes are present in eukaryotes: nitrate reductase (NR), sulfite oxidase (SO), aldehyde oxidase (AO), xanthine oxidase (XO) and the amidoxime-reducing component (mARC). Cells acquire Mo in form of the oxyanion molybdate using specific molybdate transporters. In bacteria, molybdate transport is an extensively studied process and is mediated mainly by the ATP-binding cassette system ModABC. In contrast, in eukaryotes, molybdate transport is poorly understood since specific molybdate transporters remained unknown until recently. Two rather distantly related families of proteins, MOT1 and MOT2, are involved in eukaryotic molybdate transport. They each feature high-affinity molybdate transporters that regulate the intracellular concentration of Mo and thus control activity of Mo-enzymes. The present chapter presents an overview of the biological functions of Mo with special focus on recent data related to its uptake, binding and storage.

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