X-ray crystal structure and EPR spectra of "arsenite-inhibited" Desulfovibriogigas aldehyde dehydrogenase: a member of the xanthine oxidase family

X-ray crystallography has been used to determine the structure of arsenite-inhibited aldehyde dehydrogenase from Desulfovibrio gigas, a member of the xanthine oxidase family of mononuclear molybdenum enzymes. The structure shows an AsO3 moiety bound to the molybdenum atom of the active site through...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2004-07, Vol.126 (28), p.8614-8615
Main Authors: Boer, D Roeland, Thapper, Anders, Brondino, Carlos D, Romão, Maria J, Moura, José J G
Format: Article
Language:English
Subjects:
Aldehyde Oxidoreductases - antagonists & inhibitors
Aldehyde Oxidoreductases - chemistry
Aldehyde Oxidoreductases - metabolism
Arsenites - metabolism
Arsenites - pharmacology
Crystallography, X-Ray
Desulfovibrio gigas - enzymology
Electron Spin Resonance Spectroscopy - methods
Ligands
Molecular Structure
Molybdenum - chemistry
Oxidation-Reduction
Xanthine Oxidase - antagonists & inhibitors
Xanthine Oxidase - chemistry
Xanthine Oxidase - metabolism
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Summary:X-ray crystallography has been used to determine the structure of arsenite-inhibited aldehyde dehydrogenase from Desulfovibrio gigas, a member of the xanthine oxidase family of mononuclear molybdenum enzymes. The structure shows an AsO3 moiety bound to the molybdenum atom of the active site through one of the oxygen atoms. A reduced sample of arsenite-inhibited aldehyde dehydrogenase has a Mo(V) signal that shows anisotropic hyperfine and quadrupole coupling to one arsenic atom. This signal has a strong resemblance with a previously reported signal for arsenite-inhibited xanthine oxidase.
ISSN:0002-7863