The active site of arsenite oxidase from Alcaligenes faecalis

被引:52
作者
Conrads, T
Hemann, C
George, GN
Pickering, IJ
Prince, RC
Hille, R
机构
[1] Stanford Linear Accelerator Ctr, Stanford Synchrotron Radiat Lab, Menlo Pk, CA 94025 USA
[2] Ohio State Univ, Dept Biochem, Columbus, OH 43210 USA
[3] Exxon Res & Engn Co, Annandale, NJ 08801 USA
关键词
D O I
10.1021/ja027684q
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Arsenite oxidase, a member of the DMSO reductase family of molybdenum enzymes, has two molecules of guanosine dinucleotide molybdenum cofactor coordinating the molybdenum at the active site. X-ray absorption spectroscopy indicates that the Mo-S bonds shorten from 2.47 to 2.37 Å upon reduction with the physiological substrate. It also indicates the presence of an oxo ligand at 1.70 Å in both oxidized and reduced forms of the enzyme, together with a short, 1.83 Å, Mo-O bond in the oxidized form that is lost upon reduction. Resonance Raman spectroscopy indicates that the two pterin dithiolene moieties have different aromaticities, with one, the Q-pterin, having a more discrete dithiolate structure while the other, the P-pterin, has considerable π-delocalization. Our results indicate that the structure of arsenite oxidase is intermediate between that seen in other molybdenum enzymes, in which one ligand to the metal is provided by the polypeptide (serine, cysteine, or selenocysteine), and tungsten enzymes that lack a peptide ligand. Copyright © 2002 American Chemical Society.
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页码:11276 / 11277
页数:2
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