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

D. Roeland Boer, Anders Thapper, Carlos D. Brondino, Maria J. Romão, José J. G. Moura

Research output: Contribution to journalArticlepeer-review

28 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)8614-8615
Number of pages2
JournalJournal of the American Chemical Society
Volume126
Issue number28
DOIs
Publication statusPublished - 21 Jul 2004

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