The active sites of molybdenum- and tungsten-containing enzymes

Protein X-ray crystallography has revealed the structures of the active sites of several molybdenum- and tungsten-containing enzymes that catalyze formal hydroxylation and oxygen atom transfer reactions. Each molybdenum (or tungsten) atom is coordinated by one (or two) ene-dithiolate groups of a nov...

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Bibliographic Details
Published in:Current opinion in chemical biology 1998-04, Vol.2 (2), p.201-207
Main Authors: McMaster, J, Enemark, John H
Format: Article
Language:English
Subjects:
Aldehyde Oxidoreductases - chemistry
Bacterial Proteins - chemistry
Binding Sites - physiology
Coenzymes
Iron-Sulfur Proteins
Metalloproteins - chemistry
Models, Molecular
Molybdenum - physiology
Oxidoreductases - chemistry
Oxidoreductases Acting on Sulfur Group Donors - chemistry
Pteridines - chemistry
Tungsten - physiology
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Summary:Protein X-ray crystallography has revealed the structures of the active sites of several molybdenum- and tungsten-containing enzymes that catalyze formal hydroxylation and oxygen atom transfer reactions. Each molybdenum (or tungsten) atom is coordinated by one (or two) ene-dithiolate groups of a novel pterin (molybdopterin), and the active sites are further differentiated from one another by the number of acid residues. These active-site structures have no precedent in the coordination chemistry of molybdenum and tungsten.
ISSN:1367-5931
1879-0402
DOI:10.1016/S1367-5931(98)80061-6