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JXB Advance Access originally published online on March 9, 2007
Journal of Experimental Botany 2007 58(9):2289-2296; doi:10.1093/jxb/erm024
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© The Author [2007]. Published by Oxford University Press [on behalf of the Society for Experimental Biology]. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

RESEARCH PAPER

Biology of the molybdenum cofactor

Ralf R. Mendel*

Institute of Plant Biology, Technical University of Braunschweig, 38106 Braunschweig, Germany

* To whom correspondence should be addressed. E-mail: r.mendel{at}tu-bs.de

The transition element molybdenum (Mo) is an essential micronutrient for plants where it is needed as a catalytically active metal during enzyme catalysis. Four plant enzymes depend on molybdenum: nitrate reductase, sulphite oxidase, xanthine dehydrogenase, and aldehyde oxidase. However, in order to gain biological activity and fulfil its function in enzymes, molybdenum has to be complexed by a pterin compound thus forming the molybdenum cofactor. In this article, the path of molybdenum from its uptake into the cell, via formation of the molybdenum cofactor and its storage, to the final modification of the molybdenum cofactor and its insertion into apo-metalloenzymes will be reviewed.

Key words: Aldehyde oxidase, Arabidopsis thaliana, molybdenum cofactor, nitrate reductase, sulphite oxidase, xanthine dehydrogenase

Received 1 December 2006; Revised 23 January 2007 Accepted 23 January 2007


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