The CO and CN- ligands to the active site Fe in [NiFe]-hydrogenase of Escherichia coli have different metabolic origins
The CO and CN- ligands to the active site Fe in [NiFe]-hydrogenase of Escherichia coli have different metabolic origins
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DOI：
10.1016/j.febslet.2007.06.028
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发表时间：
2007-07-10
期刊：
影响因子：
3.5
通讯作者：
Sawers, R. Gary
中科院分区：
文献类型：
--
作者：
Forzi, Lucia;Hellwig, Petra;Sawers, R. Gary
竖棒状NiFe竖棒状氢化酶的双金属活性位点上的铁原子有一个CO和两个氰化物配体。为了确定它们的代谢来源，从l -立棒uredo - c -13立棒柑桔碱培养的大肠杆菌中分离出立棒NiFe立棒氢化酶-2，纯化并进行红外光谱分析。光谱显示C-13只与氰化物配体结合，而没有与CO结合，表明氰化物和CO具有不同的代谢来源。大肠杆菌在(CO)-C-13存在下生长后，只有CO配体被13C标记。标记不是由内在的CO配体与外源的CO交换产生的。(C) 2007年由爱思唯尔B.V.代表欧洲生化学会联合会发表。
The Fe atom in the bimetallic active site of vertical bar NiFe vertical bar-hydrogenases has one CO and two cyanide ligands. To determine their metabolic origin, vertical bar NiFe vertical bar-hydrogenase-2 was isolated from Escherichia coli grown in the presence of L-vertical bar ureido-C-13 vertical bar citruiline, purified and analyzed bay infrared spectroscopy. The spectra indicate incorporation of C-13 only into the cyanide ligands and not into the CO, showing that cyanide and CO have different metabolic origins. After growth of E. coli in the presence of (CO)-C-13 only the CO ligand was labelled with 13C. Labelling did not result from an exchange of the intrinsic CO ligand with the exogenous CO. (C) 2007 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.