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Biology of the molybdenum cofactor
Author(s) -
Ralf R. Mendel
Publication year - 2007
Publication title -
journal of experimental botany
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.616
H-Index - 242
eISSN - 1460-2431
pISSN - 0022-0957
DOI - 10.1093/jxb/erm024
Subject(s) - molybdenum cofactor , molybdenum , pterin , aldehyde oxidase , cofactor , sulfite oxidase , chemistry , xanthine oxidase , enzyme , nitrate reductase , xanthine dehydrogenase , biochemistry , inorganic chemistry
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.

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