Cell biology of molybdenum in plants

Plant Cell Reports
R R Mendel

Abstract

The transition element molybdenum (Mo) is of essential importance for (nearly) all biological systems as it is required by enzymes catalyzing important reactions within the cell. The metal itself is biologically inactive unless it is complexed by a special cofactor. With the exception of bacterial nitrogenase, where Mo is a constituent of the FeMo-cofactor, Mo is bound to a pterin, thus forming the molybdenum cofactor (Moco) which is the active compound at the catalytic site of all other Mo-enzymes. In plants, the most prominent Mo-enzymes are nitrate reductase, sulfite oxidase, xanthine dehydrogenase, aldehyde oxidase, and the mitochondrial amidoxime reductase. The biosynthesis of Moco involves the complex interaction of six proteins and is a process of four steps, which also includes iron as well as copper in an indispensable way. After its synthesis, Moco is distributed to the apoproteins of Mo-enzymes by Moco-carrier/binding proteins that also participate in Moco-insertion into the cognate apoproteins. Xanthine dehydrogenase and aldehyde oxidase, but not the other Mo-enzymes, require a final step of posttranslational activation of their catalytic Mo-center for becoming active.

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Mar 27, 2012·Journal of Experimental Botany·Yoshihiro Mano, Keiichirou Nemoto
Jul 19, 2012·PLoS Genetics·Seifollah Poormohammad KianiOlivier Loudet
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Feb 19, 2015·Toxicology and Industrial Health·Hong-Wei WangEr-Jie Tian

Related Concepts

Molybdenum cofactor
Coenzymes
Metalloproteins
Molybdenum
Pteridinones
Xanthine Dehydrogenase
Mitochondrial Proteins
Aldehyde oxidase
Sulfite Oxidase
Nitrate reductase

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