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Pyranopterin conformation defines the function of molybdenum and tungsten enzymes
- Source :
- Proceedings of the National Academy of Sciences of the United States of America. 109(37)
- Publication Year :
- 2012
-
Abstract
- We have analyzed the conformations of 319 pyranopterins in 102 protein structures of mononuclear molybdenum and tungsten enzymes. These span a continuum between geometries anticipated for quinonoid dihydro, tetrahydro, and dihydro oxidation states. We demonstrate that pyranopterin conformation is correlated with the protein folds defining the three major mononuclear molybdenum and tungsten enzyme families, and that binding-site micro-tuning controls pyranopterin oxidation state. Enzymes belonging to the bacterial dimethyl sulfoxide reductase (DMSOR) family contain a metal-bis-pyranopterin cofactor, the two pyranopterins of which have distinct conformations, with one similar to the predicted tetrahydro form, and the other similar to the predicted dihydro form. Enzymes containing a single pyranopterin belong to either the xanthine dehydrogenase (XDH) or sulfite oxidase (SUOX) families, and these have pyranopterin conformations similar to those predicted for tetrahydro and dihydro forms, respectively. This work provides keen insight into the roles of pyranopterin conformation and oxidation state in catalysis, redox potential modulation of the metal site, and catalytic function.
- Subjects :
- Iron-Sulfur Proteins
Models, Molecular
Protein Folding
Stereochemistry
Xanthine Dehydrogenase
chemistry.chemical_element
Redox
Cofactor
Tungsten
chemistry.chemical_compound
Protein structure
Sulfite oxidase
polycyclic compounds
Organic chemistry
heterocyclic compounds
chemistry.chemical_classification
Molybdenum
Multidisciplinary
Crystallography
biology
Molecular Structure
Chemistry
Sulfite Oxidase
Enzymes
Pterins
Enzyme
Xanthine dehydrogenase
Physical Sciences
biology.protein
Protein folding
Oxidoreductases
Oxidation-Reduction
Subjects
Details
- ISSN :
- 10916490
- Volume :
- 109
- Issue :
- 37
- Database :
- OpenAIRE
- Journal :
- Proceedings of the National Academy of Sciences of the United States of America
- Accession number :
- edsair.doi.dedup.....11c93aefc12270fdbebf0627f889d503