Cell biology of molybdenum

Biofactors. 2009 Sep-Oct;35(5):429-34. doi: 10.1002/biof.55.


The transition element molybdenum (Mo) is an essential micronutrient that is needed as catalytically active metal during enzyme catalysis. In humans four enzymes depend on Mo: sulfite oxidase, xanthine oxidoreductase, aldehyde oxidase, and mitochondrial amidoxime reductase. In addition to these enzymes, plants harbor a fifth Mo-enzyme namely nitrate reductase. To gain biological activity and fulfill its function in enzymes, Mo has to be complexed by a pterin compound thus forming the molybdenum cofactor. This article will review the way that Mo takes from uptake into the cell, via formation of the molybdenum cofactor and its storage, up to the final insertion of the molybdenum cofactor into apometalloenzymes.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Aldehyde Oxidase / metabolism*
  • Coenzymes / biosynthesis
  • Coenzymes / metabolism*
  • Humans
  • Metalloproteins / biosynthesis
  • Metalloproteins / metabolism*
  • Molybdenum / metabolism
  • Molybdenum / physiology*
  • Molybdenum Cofactors
  • Nitrate Reductase / metabolism
  • Oxidoreductases / metabolism
  • Pteridines / metabolism*
  • Sulfite Oxidase / metabolism*
  • Sulfurtransferases / metabolism
  • Xanthine Dehydrogenase / metabolism*


  • Coenzymes
  • Metalloproteins
  • Molybdenum Cofactors
  • Pteridines
  • Molybdenum
  • molybdenum cofactor
  • Oxidoreductases
  • amidoxime reducing component, human
  • Xanthine Dehydrogenase
  • Aldehyde Oxidase
  • Nitrate Reductase
  • Sulfite Oxidase
  • MOCOS protein, human
  • Sulfurtransferases