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The active sites of molybdenum- and tungsten-containing enzymes
- Source :
- Current Opinion in Chemical Biology. 2:201-207
- Publication Year :
- 1998
- Publisher :
- Elsevier BV, 1998.
-
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.
- Subjects :
- Iron-Sulfur Proteins
Models, Molecular
inorganic chemicals
Stereochemistry
Coenzymes
chemistry.chemical_element
Tungsten
Photochemistry
Biochemistry
Cofactor
Analytical Chemistry
Coordination complex
Hydroxylation
chemistry.chemical_compound
Bacterial Proteins
Metalloproteins
Oxidoreductases Acting on Sulfur Group Donors
Pterin
Molybdenum
chemistry.chemical_classification
Binding Sites
biology
Pteridines
Molybdopterin
equipment and supplies
Aldehyde Oxidoreductases
Enzyme
chemistry
biology.protein
bacteria
Oxidoreductases
Molybdenum Cofactors
Subjects
Details
- ISSN :
- 13675931
- Volume :
- 2
- Database :
- OpenAIRE
- Journal :
- Current Opinion in Chemical Biology
- Accession number :
- edsair.doi.dedup.....93e6ce987fd65f79a3ea79a4abd20347