Molybdenum cofactors, enzymes and pathways

Günter Schwarz, Ralf R. Mendel and Markus W. Ribbe
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Günter Schwarz: Institute of Biochemistry, University of Cologne
Ralf R. Mendel: Institute of Plant Biology, Braunschweig University of Technology
Markus W. Ribbe: School of Biological Sciences, University of California

Nature, 2009, vol. 460, issue 7257, 839-847

Abstract: Abstract The trace element molybdenum is essential for nearly all organisms and forms the catalytic centre of a large variety of enzymes such as nitrogenase, nitrate reductases, sulphite oxidase and xanthine oxidoreductases. Nature has developed two scaffolds holding molybdenum in place, the iron–molybdenum cofactor and pterin-based molybdenum cofactors. Despite the different structures and functions of molybdenum-dependent enzymes, there are important similarities, which we highlight here. The biosynthetic pathways leading to both types of cofactor have common mechanistic aspects relating to scaffold formation, metal activation and cofactor insertion into apoenzymes, and have served as an evolutionary 'toolbox' to mediate additional cellular functions in eukaryotic metabolism.

Date: 2009
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DOI: 10.1038/nature08302

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