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 novel pterin (molybdopterin), and the active sites are further differentiated from one another by the number of terminal oxo and/or sulfido groups and by coordinated amino acid residues. These active-site structures have no precedent in the coordination chemistry of molybdenum and tungsten.
McMaster
J
J
Department of Chemistry, University of Arizona, Tucson, AZ 85721, USA. mcmaster@u.arizona.edu
Enemark
J H
JH
D000445:Aldehyde Oxidoreductases / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry; D001665:Binding Sites / Q000502:physiology*; D003067:Coenzymes; D007506:Iron-Sulfur Proteins; D008667:Metalloproteins / Q000737:chemistry*; D008958:Models, Molecular; D008982:Molybdenum / Q000502:physiology*; D000090006:Molybdenum Cofactors; D010088:Oxidoreductases / Q000737:chemistry; D050862:Oxidoreductases Acting on Sulfur Group Donors / Q000737:chemistry; D011621:Pteridines / Q000737:chemistry; D014414:Tungsten / Q000502:physiology*
D000445:Aldehyde Oxidoreductases; D001426:Bacterial Proteins; D003067:Coenzymes; D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D008982:Molybdenum; D000090006:Molybdenum Cofactors; D010088:Oxidoreductases; D050862:Oxidoreductases Acting on Sulfur Group Donors; D011621:Pteridines; D014414:Tungsten; C022261:molybdopterin; C080010:aldehyde ferredoxin oxidoreductase; C045664:dimethyl sulfoxide reductase