INVESTIGADORES
BRONDINO Carlos Dante
artículos
Título:
-ray crystal structure and EPR-spectra of arsenite-inhibited Desulfovibrio gigas aldehyde dehydrogenase; a member of the xanthine oxidase family
Autor/es:
D. R. BOER; A. THAPPER; C. D. BRONDINO; J. J. G. MOURA; M. J. ROMÃO
Revista:
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Editorial:
American Chemical Society
Referencias:
Año: 2004 vol. 126 p. 8614 - 8615
ISSN:
0002-7863
Resumen:
Aldehyde dehydrogenase (ADH, or aldehyde oxidoreductase, also known as MOP) from DesulfoVibrio gigas belongs to the xanthine oxidase (XO) family of mononuclear molybdenum enzymes. The inhibition of XO by arsenite was reported over 70 years ago and has been studied extensively. This work presents the first molecular structure of an arsenite-inhibited complex of a member of the XO family and the EPR properties of a paramagnetic species detected in the reduced form of the active enzyme in the presence of arsenite.
