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

被引：28

作者：

Boer, DR

Thapper, A

Brondino, CD

Romao, MJ ^{[1
]}

Moura, JJG

机构：

[1] Univ Nova Lisboa, Fac Ciencias & Tecnol, CQFB, REQUIMTE Dept Quim, P-2829516 Caparica, Portugal

[2] Univ Nacl Litoral, Fac Bioquim & Ciencias Biol, Santa Fe, Argentina

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2004年 / 126卷 / 28期

关键词：

D O I：

10.1021/ja0490222

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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. Copyright © 2004 American Chemical Society.

引用

页码：8614 / 8615

页数：2

共 19 条

[1]

BARREY G, 1928, BIOCHEM J, V22, P1101

[2]

COUGHLAN MP, 1969, J BIOL CHEM, V244, P2658

[3] ARSENITE-INHIBITED XANTHINE-OXIDASE - DETERMINATION OF THE MO-S-AS GEOMETRY BY EXAFS [J].