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Issue 21, 2009
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Molybdenum and tungsten enzymes: a crystallographic and mechanistic overview

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Abstract

Molybdenum and tungsten enzymes which contain the pyranopterin cofactor are ubiquitous in Nature and perform a wide variety of biological functions. They catalyze a diversity of mostly two-electron oxidationreduction reactions crucial in the metabolism of nitrogen, sulfur and carbon. These enzymes share common structural features, but reveal different polypeptide folding topologies and different active site coordination geometries, which, in part, dictate their function and specificity. On the basis of structural, spectroscopic and biochemical characteristics, they have been classified into three broad families named according to well-studied enzymes of each family: xanthine oxidase, sulfite oxidase and DMSO reductase. An overview of the X-ray crystallography data for representative members of the three enzyme families is given here, focusing on the mechanistic implications drawn from the structural data.

Graphical abstract: Molybdenum and tungsten enzymes: a crystallographic and mechanistic overview

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Publication details

The article was received on 25 Nov 2008, accepted on 20 Feb 2009 and first published on 14 Mar 2009


Article type: Perspective
DOI: 10.1039/B821108F
Citation: Dalton Trans., 2009, 4053-4068
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    Molybdenum and tungsten enzymes: a crystallographic and mechanistic overview

    M. J. Romão, Dalton Trans., 2009, 4053
    DOI: 10.1039/B821108F

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