X-ray Crystal Structure and EPR Spectra of “Arsenite-Inhibited” Desulfovibrio gigas 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 AsO sub(3) moiety bound to the molybdenum atom of the active site th...

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Veröffentlicht in:	Journal of the American Chemical Society 2004-07, Vol.126 (28), p.8614-8615
Hauptverfasser:	BOER, D. Roeland, THAPPER, Anders, BRONDINO, Carlos D., ROMãO, Maria J., MOURA, José J. G.
Format:	Artikel
Sprache:	eng
Schlagworte:	Biological and medical sciences Crystalline structure Desulfovibrio gigas Fundamental and applied biological sciences. Psychology Molecular biophysics Structure in molecular biology
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Zusammenfassung:	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 AsO sub(3) 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 1520-5126
DOI:	10.1021/ja0490222