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Cell biology of molybdenum
Author(s) -
Mendel Ralf R.
Publication year - 2009
Publication title -
biofactors
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.204
H-Index - 94
eISSN - 1872-8081
pISSN - 0951-6433
DOI - 10.1002/biof.55
Subject(s) - sulfite oxidase , molybdenum cofactor , pterin , molybdenum , aldehyde oxidase , cofactor , enzyme , chemistry , xanthine oxidase , nitrate reductase , biochemistry , reductase , catalysis , oxidoreductase , inorganic chemistry
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. © 2009 International Union of Biochemistry and Molecular Biology, Inc.