Abstract
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.
Publication types
-
Research Support, U.S. Gov't, P.H.S.
-
Review
MeSH terms
-
Aldehyde Oxidoreductases / chemistry
-
Bacterial Proteins / chemistry
-
Binding Sites / physiology*
-
Coenzymes*
-
Iron-Sulfur Proteins*
-
Metalloproteins / chemistry*
-
Models, Molecular
-
Molybdenum / physiology*
-
Molybdenum Cofactors
-
Oxidoreductases / chemistry
-
Oxidoreductases Acting on Sulfur Group Donors / chemistry
-
Pteridines / chemistry
-
Tungsten / physiology*
Substances
-
Bacterial Proteins
-
Coenzymes
-
Iron-Sulfur Proteins
-
Metalloproteins
-
Molybdenum Cofactors
-
Pteridines
-
Molybdenum
-
molybdenum cofactor
-
Oxidoreductases
-
Aldehyde Oxidoreductases
-
aldehyde ferredoxin oxidoreductase
-
Oxidoreductases Acting on Sulfur Group Donors
-
dimethyl sulfoxide reductase
-
Tungsten