期刊
JOURNAL OF INORGANIC BIOCHEMISTRY
卷 105, 期 7, 页码 927-936出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.jinorgbio.2011.03.020
关键词
Tungstoenzyme; Formaldehyde oxidoreductase; Reaction mechanism; Density functional theory; Enzyme catalysis
资金
- Swedish Research Council [621-2009-4736, 622-2009-371]
- National Natural Science Foundation of China [20873008]
Formaldehyde ferredoxin oxidoreductase from Pyrococcus furiosus is a tungsten-dependent enzyme that catalyzes the oxidation of formaldehyde to formic acid. In the present study, quantum chemical calculations are used to elucidate the reaction mechanism of this enzyme. Several possible mechanistic scenarios are investigated with a large model of the active site designed on the basis of the X-ray crystal structure of the native enzyme. Based on the calculations, we propose a new mechanism in which the formaldehyde substrate binds directly to the tungsten ion. W-VI=O then performs a nucleophilic attack on the formaldehyde carbon to form a tetrahedral intermediate. In the second step, which is calculated to be rate limiting, a proton is transferred to the second-shell Glu308 residue, coupled with a two-electron reduction of the tungsten ion. The calculated barriers for the mechanism are energetically very feasible and in relatively good agreement with experimental rate constants. Three other second-shell mechanisms, including one previously proposed based on experimental findings, are considered but ruled out because of their high barriers. (C) 2011 Elsevier Inc. All rights reserved.
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