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Geometrical Control of the Active Site Electronic Structure of Pyranopterin Enzymes by Metal-Dithiolate Folding: Aldehyde Oxidase
- Source :
- Journal of the American Chemical Society. 126:11784-11785
- Publication Year :
- 2004
- Publisher :
- American Chemical Society (ACS), 2004.
-
Abstract
- Density functional calculations on geometry-optimized oxidized (Mo(VI)) and reduced (Mo(IV)) analogues of the isolated active site of aldehyde oxidase (MOP), a member of the xanthine oxidase family of pyranopterindithiolate enzymes, show that fold angle changes of the dithiolate ligand modulate the relative metal and dithiolate contributions to the frontier redox orbitals. Proton abstraction from the equatorial aqua ligand of the oxidized Mo(VI) site also flattens the metal dithiolate fold angle. It is proposed that static and/or dynamic changes in the structure of the protein surrounding the active site can induce changes in the dithiolate fold angle and thereby provide a mechanism for electronic buffering of the redox orbital, for fine-tuning the nucleophilicity of the equatorial aqua/hydroxide ligand, and for modulating the electron-transfer regeneration of the active sites of molybdenum and tungsten enzymes via a "dithiolate folding effect".
- Subjects :
- Models, Molecular
Protein Folding
Stereochemistry
Coenzymes
chemistry.chemical_element
Biochemistry
Redox
Catalysis
Metal
Structure-Activity Relationship
chemistry.chemical_compound
Colloid and Surface Chemistry
Nucleophile
Metalloproteins
Organometallic Compounds
Xanthine oxidase
Aldehyde oxidase
Molybdenum
Binding Sites
Sulfur Compounds
biology
Chemistry
Pteridines
Active site
General Chemistry
Aldehyde Oxidase
visual_art
biology.protein
visual_art.visual_art_medium
Hydroxide
sense organs
Molybdenum Cofactors
Subjects
Details
- ISSN :
- 15205126 and 00027863
- Volume :
- 126
- Database :
- OpenAIRE
- Journal :
- Journal of the American Chemical Society
- Accession number :
- edsair.doi.dedup.....d1ebe20044ffd49439de6fb21ee67926